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| Product | Description | |
|---|---|---|
| Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase (Crude Enzyme) | GSH, and by extension GCL, is critical to cell survival. Nearly every eukaryotic cell, from plants to yeast to humans, expresses a form of the GCL protein for the purpose of synthesizing GSH. To further highlight the critical nature of this enzyme, genetic knockdown of GCL results in embryonic lethality. Furthermore, dysregulation of GCL enzymatic function and activity is known to be involved in the vast majority of human diseases, such as diabetes, Parkinson's disease, Alzheimers disease, COPD, HIV/AIDS, and cancer. This typically involves impaired function leading to decreased GSH biosynthesis, reduced cellular antioxidant capacity, and the in...se forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Agriculture; medicine; synthesis; biotechnology; pharmacology. Group: Enzymes. Enzyme Commission Number: EC 6.3.2.2/ 6.3.2.3. CAS No. 9023-64-7/9023-62-5. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase; Glutamylcysteine Synthetase; Glutathione Synthetase. Pack: 100ml. Cat No: NATE-1859. |  |
| (13E)-labda-7,13-dien-15-ol synthase | The enzyme from the lycophyte Selaginella moellendorffii is bifunctional, initially forming (13E)-labda-7,13-dien-15-yl diphosphate, which is hydrolysed to the alcohol. Group: Enzymes. Synonyms: labda-7,13E-dien-15-ol synthase. Enzyme Commission Number: EC 3.1.7.10. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3761; (13E)-labda-7,13-dien-15-ol synthase; EC 3.1.7.10; labda-7,13E-dien-15-ol synthase. Cat No: EXWM-3761. | |
| 16S rRNA (cytidine1409-2'-O)-methyltransferase | The bifunctional enzyme from Mycobacterium tuberculosis 2'-O-methylates cytidine1409 in helix 44 of 16S rRNA and cytidine1920 in helix 69 of 23S rRNA (cf. EC 2.1.1.226, 23S rRNA (cytidine1920-2'-O)-methyltransferase). Group: Enzymes. Synonyms: TlyA (ambiguous). Enzyme Commission Number: EC 2.1.1.227. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1830; 16S rRNA (cytidine1409-2'-O)-methyltransferase; EC 2.1.1.227; TlyA (ambiguous). Cat No: EXWM-1830. | |
| 17β-estradiol 17-dehydrogenase | The enzyme oxidizes or reduces the hydroxy/keto group on C17 of estrogens and androgens in mammals and regulates the biological potency of these steroids. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase. The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, 20α-hydroxysteroid dehydrogenase, it is Si-specific with respect to NAD(P)+. Group: Enzymes. Synonyms: 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7. Enzyme Commission Number: EC 1.1.1.62. CAS No. 9028-61-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0348; 17β-estradiol 17-dehydrogenase; EC 1.1.1.62; 9028-61-9; 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7. Cat No: EXWM-0348. | |
| 1L-myo-inositol 1-phosphate cytidylyltransferase | In many organisms this activity is catalysed by a bifunctional enzyme. The cytidylyltransferase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments. Group: Enzymes. Synonyms: CTP:inositol-1-phosphate cytidylyltransferase (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); IPCT (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phospha. Enzyme Commission Number: EC 2.7.7.74. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3286; 1L-myo-inositol 1-phosphate cytidylyltransferase; EC 2.7.7.74; CTP:inositol-1-phosphate cytidylyltransferase (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); IPCT (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); L-myo-inositol-1-phosphate cytidylyltransferase. Cat No: EXWM-3286. | |
| 2,3-diketo-5-methylthiopentyl-1-phosphate enolase | The enzyme participates in the methionine salvage pathway in Bacillus subtilis.In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 3.1.3.87, 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase. Group: Enzymes. Synonyms: DK-MTP-1-P enolase; MtnW; YkrW; RuBisCO-like protein; RLP. Enzyme Commission Number: EC 5.3.2.5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5485; 2,3-diketo-5-methylthiopentyl-1-phosphate enolase; EC 5.3.2.5; DK-MTP-1-P enolase; MtnW; YkrW; RuBisCO-like protein; RLP. Cat No: EXWM-5485. | |
| 23S rRNA (cytidine1920-2'-O)-methyltransferase | The bifunctional enzyme from Mycobacterium tuberculosis 2'-O-methylates cytidine1920 in helix 69 of 23S rRNA and cytidine1409 in helix 44 of 16S rRNA (cf. EC 2.1.1.227, 16S rRNA (cytidine1409-2'-O)-methyltransferase). These methylations result in increased susceptibility to the antibiotics capreomycin and viomycin. Group: Enzymes. Synonyms: TlyA (ambiguous). Enzyme Commission Number: EC 2.1.1.226. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1829; 23S rRNA (cytidine1920-2'-O)-methyltransferase; EC 2.1.1.226; TlyA (ambiguous). Cat No: EXWM-1829. | |
| 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase | The enzyme participates in the methionine salvage pathway in Bacillus subtilis.In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 5.3.2.5, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase. Group: Enzymes. Synonyms: HK-MTPenyl-1-P phosphatase; MtnX; YkrX. Enzyme Commission Number: EC 3.1.3.87. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3693; 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; EC 3.1.3.87; HK-MTPenyl-1-P phosphatase; MtnX; YkrX. Cat No: EXWM-3693. | |
| 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase | This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant. The bifunctional enzyme from Escherichia coli also catalyses the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163). Group: Enzymes. Synonyms: ubiE (gene name, ambiguous). Enzyme Commission Number: EC 2.1.1.201. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1802; 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase; EC 2.1.1.201; ubiE (gene name, ambiguous). Cat No: EXWM-1802. | |
| 3β-hydroxy-Δ5-steroid dehydrogenase | This activity is found in several bifunctional enzymes that catalyse the oxidative conversion of Δ5-3-hydroxy steroids to a Δ4-3-oxo configuration. This conversion is carried out in two separate, sequential reactions; in the first reaction, which requires NAD+, the enzyme catalyses the dehydrogenation of the 3β-hydroxy steroid to a 3-oxo intermediate. In the second reaction the reduced coenzyme, which remains attached to the enzyme, activates the isomerization of the Δ5 form to a Δ4 form (cf. EC 5.3.3.1, steroid Δ-isomerase). Substrates include dehydroepiandrosterone (which is converted into androst-5-ene-3,17-dione), pregnenolone (co...5-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0049; 3β-hydroxy-Δ5-steroid dehydrogenase; EC 1.1.1.145; 9044-85-3; progesterone reductase; Δ5-3β-hydroxysteroid dehydrogenase; 3β-hydroxy-5-ene steroid dehydrogenase; 3β-hydroxy steroid dehydrogenase/isomerase; 3β-hydroxy-Δ5-C27-steroid dehydrogenase/isomerase; 3β-hydroxy-Δ5-C27-steroid oxidoreductase; 3β-hydroxy-5-ene-steroid oxidoreductase; steroid-Δ5-3β-ol dehydrogenase; 3β-HSDH; 5-ene-3-β-hydroxysteroid dehydrogenase; 3β-hydroxy-5-ene-steroid d | |
| 3β-hydroxysteroid 3-dehydrogenase | The enzyme acts on multiple 3β-hydroxysteroids. Participates in the biosynthesis of zemosterol and cholesterol, where it catalyses the reaction in the opposite direction to that shown. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.62, 17β-estradiol 17-dehydrogenase. Group: Enzymes. Synonyms: 3-keto-steroid reductase; 3-KSR; HSD17B7 (gene name); ERG27 (gene name). Enzyme Commission Number: EC 1.1.1.270. CAS No. 42616-29-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0177; 3β-hydroxysteroid 3-dehydrogenase; EC 1.1.1.270; 42616-29-5; 3-keto-steroid reductase; 3-KSR; HSD17B7 (gene name); ERG27 (gene name). Cat No: EXWM-0177. | |
| 3-hexulose-6-phosphate synthase | Requires Mg2+ or Mn2+ for maximal activity. The enzyme is specific for D-ribulose 5-phosphate as substrate as ribose 5-phosphate, xylulose 5-phosphate, allulose 6-phosphate and fructose 6-phosphate cannot act as substrate. In addition to formaldehyde, the enzyme can also use glycolaldehyde and methylglyoxal. This enzyme, along with EC 5.3.1.27, 6-phospho-3-hexuloisomerase, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds. The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of this enzyme and EC 5.3.1.27, 6-phospho-3-hexuloisomerase. This enzyme is a member of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily. Group: Enzymes. Synonyms: D-arabino-3-hexulose 6-phosphate formaldehyde-lyase; 3-hexulosephosphate synthase; 3-hexulose phosphate synthase; HPS. Enzyme Commission Number: EC 4.1.2.43. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4879; 3-hexulose-6-phosphate synthase; EC 4.1.2.43; D-arabino-3-hexulose 6-phosphate formaldehyde-lyase; 3-hexulosephosphate synthase; 3-hexulose phosphate synthase; HPS. Cat No: EXWM-4879. | |
| 3-hydroxypropionate dehydrogenase (NADP+) | Catalyses the reduction of malonate semialdehyde to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75. Different from EC 1.1.1.59 [3-hydroxypropionate dehydrogenase (NAD+)] by cofactor preference. Group: Enzymes. Synonyms: 3-hydroxypropanoate dehydrogenase (NADP+); 3-hydroxypropionate:NADP+ oxidoreductase. Enzyme Commission Number: EC 1.1.1.298. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0207; 3-hydroxypropionate dehydrogenase (NADP+); EC 1.1.1.298; 3-hydroxypropanoate dehydrogenase (NADP+); 3-hydroxypropionate:NADP+ oxidoreductase. Cat No: EXWM-0207. | |
| 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase | The enzyme from Escherichia coli is a bifunctional fusion protein that also catalyses EC 3.3.2.12, oxepin-CoA hydrolase. Combined the two activities result in a two-step conversion of oxepin-CoA to 3-oxo-5,6-dehydrosuberyl-CoA, part of an aerobic phenylacetate degradation pathway. Group: Enzymes. Synonyms: paaZ (gene name). Enzyme Commission Number: EC 1.2.1.91. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1195; 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase; EC 1.2.1.91; paaZ (gene name). Cat No: EXWM-1195. | |
| 4-hydroxy-2-oxohexanoate aldolase | Requires Mn2+ for maximal activity. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzyme forms a bifunctional complex with EC 1.2.1.87, propanal dehydrogenase (CoA-propanoylating), with a tight channel connecting the two subunits. Group: Enzymes. Synonyms: BphI. Enzyme Commission Number: EC 4.1.3.43. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4920; 4-hydroxy-2-oxohexanoate aldolase; EC 4.1.3.43; BphI. Cat No: EXWM-4920. | |
| 4-hydroxy-2-oxovalerate aldolase | Requires Mn2+ for maximal activity. The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH. In some bacterial species the enzyme forms a bifunctional complex with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase. Group: Enzymes. Synonyms: 4-hydroxy-2-ketovalerate aldolase; HOA; DmpG; 4-hydroxy-2-oxovalerate pyruvate-lyase; 4-hydroxy-2-oxopentanoate pyruvate-lyase; BphI; 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Enzyme Commission Number: EC 4.1.3.39. CAS No. 37325-52-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4915; 4-hydroxy-2-oxovalerate aldolase; EC 4.1.3.39; 37325-52-3; 4-hydroxy-2-ketovalerate aldolase; HOA; DmpG; 4-hydroxy-2-oxovalerate pyruvate-lyase; 4-hydroxy-2-oxopentanoate pyruvate-lyase; BphI; 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Cat No: EXWM-4915. | |
| 6-phospho-3-hexuloisomerase | This enzyme, along with EC 4.1.2.43, 3-hexulose-6-phosphate synthase, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds. The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of EC 4.1.2.43 (3-hexulose-6-phosphate synthase) and this enzyme. Group: Enzymes. Synonyms: 3-hexulose-6-phosphate isomerase; phospho-3-hexuloisomerase; PHI; 6-phospho-3-hexulose isomerase; YckF. Enzyme Commission Number: EC 5.3.1.27. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5466; 6-phospho-3-hexuloisomerase; EC 5.3.1.27; 3-hexulose-6-phosphate isomerase; phospho-3-hexuloisomerase; PHI; 6-phospho-3-hexulose isomerase; YckF. Cat No: EXWM-5466. | |
| 8-oxo-dGDP phosphatase | The enzyme catalyses the hydrolysis of both 8-oxo-dGDP and 8-oxo-GDP thereby preventing translational errors caused by oxidative damage. The preferred in vivo substrate is not known. The enzyme does not degrade 8-oxo-dGTP and 8-oxo-GTP to the monophosphates (cf. EC 3.6.1.55, 8-oxo-dGTP diphosphatase). Ribonucleotide diphosphates and deoxyribonucleotide diphosphates are hydrolysed with broad specificity. The bifunctional enzyme NUDT5 also hydrolyses ADP-ribose to AMP and D-ribose 5-phosphate (cf. EC 3.6.1.13, ADP-ribose diphosphatase). The human enzyme NUDT18 also hydrolyses 8-oxo-dADP and 2-hydroxy-dADP, the latter at a slower rate. Group: Enzymes. Synonyms: NUDT5; MTH3 (gene name); NUDT18. Enzyme Commission Number: EC 3.6.1.58. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4630; 8-oxo-dGDP phosphatase; EC 3.6.1.58; NUDT5; MTH3 (gene name); NUDT18. Cat No: EXWM-4630. | |
| 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase | The enzyme contains heme. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60, linoleate 8R-lipoxygenase), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate within the C-terminal P-450 heme thiolate domain. Group: Enzymes. Synonyms: 5,8-LDS (bifunctional enzyme); 5,8-linoleate diol synthase (bifunctional enzyme); 8-hydroperoxide isomerase; (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate-forming); PpoA. Enzyme Commission Number: EC 5.4.4.5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5546; 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase; EC 5.4.4.5; 5,8-LDS (bifunctional enzyme); 5,8-linoleate diol synthase (bifunctional enzyme); 8-hydroperoxide isomerase; (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate-forming); PpoA. Cat No: EXWM-5546. | |
| 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase | The enzyme contains heme. The bifunctional enzyme from Gaeumannomyces graminis catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60, linoleate 8R-lipoxygenase), which is then isomerized to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate. Group: Enzymes. Synonyms: 8-hydroperoxide isomerase (ambiguous); (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate-forming). Enzyme Commission Number: EC 5.4.4.6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5547; 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase; EC 5.4.4.6; 8-hydroperoxide isomerase (ambiguous); (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate-forming). Cat No: EXWM-5547. | |
| abieta-7,13-diene synthase | Part of a bifunctional enzyme involved in the biosynthesis of abietadiene. See also EC 5.5.1.12, copalyl diphosphate synthase. Requires Mg2+. Group: Enzymes. Synonyms: copalyl-diphosphate diphosphate-lyase (cyclizing) (ambiguous); abietadiene synthase (ambiguous). Enzyme Commission Number: EC 4.2.3.18. CAS No. 157972-08-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5174; abieta-7,13-diene synthase; EC 4.2.3.18; 157972-08-2; copalyl-diphosphate diphosphate-lyase (cyclizing) (ambiguous); abietadiene synthase (ambiguous). Cat No: EXWM-5174. | |
| acetaldehyde dehydrogenase (acetylating) | Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower. Group: Enzymes. Synonyms: aldehyde dehydrogenase (acylating); ADA; acylating acetaldehyde dehyrogenase; DmpF; BphJ. Enzyme Commission Number: EC 1.2.1.10. CAS No. 9028-91-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1116; acetaldehyde dehydrogenase (acetylating); EC 1.2.1.10; 9028-91-5; aldehyde dehydrogenase (acylating); ADA; acylating acetaldehyde dehyrogenase; DmpF; BphJ. Cat No: EXWM-1116. | |
| acireductone synthase | This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one. The acireductone represents a branch point in the methione-salvage pathway as it is used in the formation of formate, CO and 3-(methylthio)propanoate by EC 1.13.11.53 [acireductone dioxygenase (Ni2+-requiring)] and of formate and 4-methylthio-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54 {acireductone dioxygenase [iron(II)-requiring]}. Group: Enzymes. Synonyms: E1; E-1 enolase-phosphatase. Enzyme Commission Number: EC 3.1.3.77. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3682; acireductone synthase; EC 3.1.3.77; E1; E-1 enolase-phosphatase. Cat No: EXWM-3682. | |
| aclacinomycin-A oxidase | A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A (cf. EC 1.1.3.45) and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y. Group: Enzymes. Synonyms: AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Enzyme Commission Number: EC 1.3.3.14. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1375; aclacinomycin-A oxidase; EC 1.3.3.14; AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Cat No: EXWM-1375. | |
| aclacinomycin-N oxidase | A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y (cf. EC 1.3.3.14, aclacinomycin A oxidase). Group: Enzymes. Synonyms: AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Enzyme Commission Number: EC 1.1.3.45. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0418; aclacinomycin-N oxidase; EC 1.1.3.45; AknOx (ambiguous); aclacinomycin oxidoreductase (ambiguous). Cat No: EXWM-0418. | |
| adenosylcobinamide-GDP ribazoletransferase | In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyse reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, α-ribazole. The second branch of the nucleotide loop assembly pathway is the cobinamide activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme Cob U. CobS catalyses the final step in adenosylcobalamin biosynthesis, which is the condensation of AdoCbi-GDP with α-ribazole to yield adenosylcobalamin. Group: Enzymes. Synonyms: CobS; cobalamin synthase; cobalamin-5'-phosphate synthase; cobalamin (5'-phosphate) synthase. Enzyme Commission Number: EC 2.7.8.26. CAS No. 137672-85-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3325; adenosylcobinamide-GDP ribazoletransferase; EC 2.7.8.26; 137672-85-6; CobS; cobalamin synthase; cobalamin-5'-phosphate synthase; cobalamin (5'-phosphate) synthase. Cat No: EXWM-3325. | |
| adenosylcobinamide-phosphate guanylyltransferase | In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyse reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, α-ribazole. The second branch of the nuclotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme Cob U. Th...s a two-stage reaction with formation of a CobU-GMP intermediate. Guanylylation takes place at histidine-46. Group: Enzymes. Synonyms: CobU; adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; AdoCbi kinase/AdoCbi-phosphate guanylyltransferase. Enzyme Commission Number: EC 2.7.7.62. CAS No. 169592-55-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3274; adenosylcobinamide-phosphate guanylyltransferase; EC 2.7.7.62; 169592-55-6; CobU; adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; AdoCbi kinase/AdoCbi-phosphate guanylyltransferas | |
| adenylyl-sulfate kinase | The human phosphoadenosine-phosphosulfate synthase (PAPSS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25). Group: Enzymes. Synonyms: adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; . Enzyme Commission Number: EC 2.7.1.25. CAS No. 9012-38-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3055; adenylyl-sulfate kinase; EC 2.7.1.25; 9012-38-8; adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; adenosine-5'-phosphosulfate-3'-phosphokinase; APS kinase. Cat No: EXWM-3055. | |
| aldos-2-ulose dehydratase | This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. Aldose-2-uloses such as 2-dehydroglucose can also act as substrates, but more slowly. This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction (1a), is inhibited by its product and requires metal ions for activity. Group: Enzymes. Synonyms: pyranosone dehydratase; AUDH; 1,5-anhydro-D-fructose dehydratase (microthecin-forming). Enzyme Commission Number: EC 4.2.1.110. CAS No. 101920-80-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4950; aldos-2-ulose dehydratase; EC 4.2.1.110; 101920-80-3; pyranosone dehydratase; AUDH; 1,5-anhydro-D-fructose dehydratase (microthecin-forming). Cat No: EXWM-4950. | |
| aminoglycoside 2''-phosphotransferase | Requires Mg2+. This bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2'', including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin. In most, but not all, cases the phosphorylation confers resistance against the antibiotic. Some forms of the enzyme use ATP as a phosphate donor in appreciable amount. The enzyme is often found as a bifunctional enzyme that also catalyses 6'-aminoglycoside N-acetyltransferase activity. The bifunctional enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci. Group: Enzymes. Synonyms: aphD (gene name); APH(2''); aminoglycoside (2'') kinase; gentamicin kinase (ambiguous); gentamicin phosphotransferase (ambiguous). Enzyme Commission Number: EC 2.7.1.190. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3023; aminoglycoside 2''-phosphotransferase; EC 2.7.1.190; aphD (gene name); APH(2''); aminoglycoside (2'') kinase; gentamicin kinase (ambiguous); gentamicin phosphotransferase (ambiguous). Cat No: EXWM-3023. | |
| aminopeptidase B | Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds. This is one of the activities of the bifunctional enzyme EC 3.3.2.6 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: arylamidase II; arginine aminopeptidase; arginyl aminopeptidase; Cl--activated arginine aminopeptidase; cytosol aminopeptidase IV; L-arginine aminopeptidase. Enzyme Commission Number: EC 3.4.11.6. CAS No. 9073-92-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4027; aminopeptidase B; EC 3.4.11.6; 9073-92-1; arylamidase II; arginine aminopeptidase; arginyl aminopeptidase; Cl--activated arginine aminopeptidase; cytosol aminopeptidase IV; L-arginine aminopeptidase. Cat No: EXWM-4027. | |
| anthranilate 3-monooxygenase (FAD) | This enzyme, isolated from the bacterium Geobacillus thermodenitrificans, participates in the pathway of tryptophan degradation. The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and an FAD reductase, which ensures ample supply of FAD to the monooxygenase. Group: Enzymes. Synonyms: anthranilate 3-hydroxylase; anthranilate hydroxylase. Enzyme Commission Number: EC 1.14.14.8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0932; anthranilate 3-monooxygenase (FAD); EC 1.14.14.8; anthranilate 3-hydroxylase; anthranilate hydroxylase. Cat No: EXWM-0932. | |
| aphidicolan-16β-ol synthase | This is a bifunctional enzyme which also has EC 5.5.1.14 syn-copalyl diphosphate synthase activity. Aphidicolan-16β-ol is a precursor of aphidicolin, a specific inhibitor of DNA polymerase α (EC 2.7.7.7). Group: Enzymes. Synonyms: PbACS. Enzyme Commission Number: EC 4.2.3.42. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5201; aphidicolan-16β-ol synthase; EC 4.2.3.42; PbACS. Cat No: EXWM-5201. | |
| Aranorosin | Antibiotic. Antibacterial. Antifungal. Anticancer compound. Inhibits anti-apoptotic functions regulated by Bcl-2. Circumvents arbekacin (ABK)-resistance in MRSA by inhibiting the bifunctional enzyme AAC(6')/APH(2''). Group: Biochemicals. Grades: Highly Purified. CAS No. 117184-53-9. Pack Sizes: 250ug, 1mg. Molecular Formula: C23H33NO6. US Biological Life Sciences. |  Worldwide |
| ATIC Dimerization Inhibitor (Ac-Arg-Ph(4-NO2)-NEt2, ATIC Inhibitor, AICAR Tfase Inhibitor, AICAR Transformylase Inhibitor, AICAR Tranformylase/Inosine Monophosphate Cyclohydrolase Dimerization Inhibitor, AMPK Signaling Activator XI) | A cell-permeable dipeptide that reversibly blocks the homodimerization of aminoimidazole carboxamide ribonucleotide transformylase/inosine nomophosphate cyclohydrolase (ATIC) and inhibits its activity (Ki = 691nM, Kd = 240nM). AITC is a bifunctional enzyme that catalyzes the last two steps of de novo purine biosynthesis. Increases the intracellular levels of AICAR leading to the activation of AMP-activated protein kinase (AMPK). Shown to reduce cell viability in a dose-dependent manner. Exhibits a longer half-life and sustained AMPK activation (~24h), compared to AICA-riboside. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 10mg. Molecular Formula: C??H??N?O?. US Biological Life Sciences. | Worldwide |
| CAY10640 | Soluble epoxide hydrolase (sEH) is a bifunctional enzyme that in humans is encoded by the EPHX2 gene. sEH is a member of the epoxide hydrolase family. CAY10640 is a 1-aryl-3-(1-acylpiperidin-4-yl)urea analog that inhibits recombinant human and mouse sEH with IC50 values both equal to 0.4 nM. Synonyms: sEHi; Soluble Epoxide Hydrolase Inhibitor; CAY 10640; CAY-10640. Grades: ≥98%. CAS No. 1208549-68-1. Molecular formula: C17H20F3N3O3. Mole weight: 371.4. |  |
| CDP-L-myo-inositol myo-inositolphosphotransferase | In many organisms this activity is catalysed by a bifunctional enzyme. The di-myo-inositol-1,3'-phosphate-1'-phosphate synthase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) uses only 1L-myo-inositol 1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-1L-myo-inositol and CDP-D-myo-inositol, are recognized as alcohol donors. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3-phosphate, a widespread organic solute in microorganisms adapted to hot environments. Group: Enzymes. Synonyms: CDP-inositol:inositol-1-phosphate transferase (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); DIPPS . Enzyme Commission Number: EC 2.7.8.34. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3333; CDP-L-myo-inositol myo-inositolphosphotransferase; EC 2.7.8.34; CDP-inositol:inositol-1-phosphate transferase (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); DIPPS (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)). Cat No: EXWM-3333. | |
| cembrene C synthase | Requires Mg2+. Isolated from the bacterium Streptomyces sp. SANK 60404. This bifunctional enzyme also produces (R)-nephthenol. See EC 4.2.3.149, nephthenol synthase. Group: Enzymes. Synonyms: DtcycA (gene name). Enzyme Commission Number: EC 4.2.3.148. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5162; cembrene C synthase; EC 4.2.3.148; DtcycA (gene name). Cat No: EXWM-5162. | |
| cholesterol oxidase | Contains FAD. Cholesterol oxidases are secreted bacterial bifunctional enzymes that catalyse the first two steps in the degradation of cholesterol. The enzyme catalyses the oxidation of the 3β-hydroxyl group to a keto group, and the isomerization of the double bond in the oxidized steroid ring system from the Δ5 position to Δ6 position (cf. EC 5.3.3.1, steroid Δ-isomerase). Group: Enzymes. Synonyms: cholesterol- O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. CHOD. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0424; cholesterol oxidase; EC 1.1.3.6; 9028-76-6; cholesterol- O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase. Cat No: EXWM-0424. | |
| Cholesterol Oxidase from Microorganism | Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2. Group: Enzymes. Synonyms: Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase; EC 1.1.3.6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. Activity: 12U/mg-solid or more. Form: Freeze dried powder. Source: Microorganism. Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase; EC 1.1.3.6. Cat No: DIA-138. | |
| Cholesterol oxidase from Nocardia sp., Recombinant | Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2. Group: Enzymes. Synonyms: EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. CHOD. Activity: > 20 Units / mg. Storage: Below -20°C. Form: Lyophilized powder. Source: E. coli. Species: Nocardia sp. EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Cat No: NATE-1033. | |
| Cholesterol Oxidase from Streptomyces sp. | Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step, which is then isomerized to cholest-4-en-3-one with the release of H2O2. Group: Enzymes. Synonyms: EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Enzyme Commission Number: EC 1.1.3.6. CAS No. 9028-76-6. Activity: 15U/mg-solid or more. Storage: -20°C. Form: Freeze dried powder. Source: Streptomyces sp. EC 1.1.3.6, cholesterol-O2 oxidoreductase; 3β-hydroxy steroid oxidoreductase; 3β-hydroxysteroid:oxygen oxidoreductase; 9028-76-6. Cat No: NATE-0128. | |
| copalyl diphosphate synthase | In some plants, such as Salvia miltiorrhiza, this enzyme is monofunctional. In other plants this activity is often a part of a bifunctional enzyme. For example, in Selaginella moellendorffii this activity is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.131, miltiradiene synthase, while in the tree Abies grandis (grand fir) it is catalysed by a bifunctional enzyme that also catalyses EC 4.2.3.18, abietadiene synthase. Group: Enzymes. Synonyms: (+)-copalyl-diphosphate lyase (decyclizing). Enzyme Commission Number: EC 5.5.1.12. CAS No. 157972-08-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5613; copalyl diphosphate synthase; EC 5.5.1.12; 157972-08-2; (+)-copalyl-diphosphate lyase (decyclizing). Cat No: EXWM-5613. | |
| deacetoxycephalosporin-C hydroxylase | Requires iron(II). The enzyme can also use 3-exomethylenecephalosporin C as a substrate to form deacetoxycephalosporin C, although more slowly. In Acremonium chrysogenum, the enzyme forms part of a bifunctional protein along with EC 1.14.20.1, deactoxycephalosporin-C synthase. It is a separate enzyme in Streptomyces clavuligerus. Group: Enzymes. Synonyms: deacetylcephalosporin C synthase; 3'-methylcephem hydroxylase; DACS; DAOC hydroxylase; deacetoxycephalosporin C hydroxylase. Enzyme Commission Number: EC 1.14.11.26. CAS No. 69772-89-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0643; deacetoxycephalosporin-C hydroxylase; EC 1.14.11.26; 69772-89-0; deacetylcephalosporin C synthase; 3'-methylcephem hydroxylase; DACS; DAOC hydroxylase; deacetoxycephalosporin C hydroxylase. Cat No: EXWM-0643. | |
| D-glycero-β-D-manno-heptose 1-phosphate adenylyltransferase | The bifunctional protein hldE includes D-glycero-β-D-manno-heptose-7-phosphate kinase and D-glycero-β-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.1.167). The enzyme is involved in biosynthesis of ADP-L-glycero-β-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. Group: Enzymes. Synonyms: D-β-D-heptose 7-phosphate kinase/D-β-D-heptose 1-phosphate adenylyltransferase; D-glycero-D-manno-heptose-1β-phosphate adenylyltransferase; hldE (gene name); rfaE (gene name). Enzyme Commission Number: EC 2.7.7.70. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3282; D-glycero-β-D-manno-heptose 1-phosphate adenylyltransferase; EC 2.7.7.70; D-β-D-heptose 7-phosphate kinase/D-β-D-heptose 1-phosphate adenylyltransferase; D-glycero-D-manno-heptose-1β-phosphate adenylyltransferase; hldE (gene name); rfaE (gene name). Cat No: EXWM-3282. | |
| D-glycero-β-D-manno-heptose-7-phosphate kinase | The bifunctional protein hldE includes D-glycero-β-D-manno-heptose-7-phosphate kinase and D-glycero-β-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.7.70). The enzyme is involved in biosynthesis of ADP-L-glycero-β-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. The enzyme selectively produces D-glycero-β-D-manno-heptose 1,7-bisphosphate. Group: Enzymes. Synonyms: heptose 7-phosphate kinase; D-β-D-heptose 7-phosphotransferase; D-β-D-heptose-7-phosphate kinase; HldE1 heptokinase; glycero-manno-heptose 7-phosphate kinase; D-β-D-heptose 7-phosphate kinase/D-β-D-heptose 1-phosphate adenylyltransferase; hldE (gene name); rfaE (gene name). Enzyme Commission Number: EC 2.7.1.167. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2997; D-glycero-β-D-manno-heptose-7-phosphate kinase; EC 2.7.1.167; heptose 7-phosphate kinase; D-β-D-heptose 7-phosphotransferase; D-β-D-heptose-7-phosphate kinase; HldE1 heptokinase; glycero-manno-heptose 7-phosphate kinase; D-β-D-heptose 7-phosphate kinase/D-β-D-heptose 1-phosphate adenylyltransferase; hldE (gene name); rfaE (gene name). Cat No: EXWM-2997. | |
| diacylglycerol diphosphate phosphatase | The bifunctional enzyme catalyses the dephosphorylation of diacylglycerol diphosphate to phosphatidate and the subsequent dephosphorylation of phosphatidate to diacylglycerol (cf. phosphatidate phosphatase (EC 3.1.3.4)). It regulates intracellular levels of diacylglycerol diphosphate and phosphatidate, phospholipid molecules believed to play a signalling role in stress response. The phosphatase activity of the bifunctional enzyme is Mg2+-independent and N-ethylmaleimide-insensitive and is distinct from the Mg2+-dependent and N-ethylmaleimide-sensitive enzyme EC 3.1.3.4 (phosphatidate phosphatase).The diacylglycerol pyrophosphate phosphatase activity in Saccharomyces cerevisiae is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase. Group: Enzymes. Synonyms: DGPP phosphatase; DGPP phosphohydrolase; DPP1; DPPL1; DPPL2; PAP2; pyrophosphate phosphatase. Enzyme Commission Number: EC 3.1.3.81. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3687; diacylglycerol diphosphate phosphatase; EC 3.1.3.81; DGPP phosphatase; DGPP phosphohydrolase; DPP1; DPPL1; DPPL2; PAP2; pyrophosphate phosphatase. Cat No: EXWM-3687. | |
| D-malate dehydrogenase (decarboxylating) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-malate:NAD+ oxidoreductase (decarboxylating). Other names in common use include D-malate dehydrogenase, D-malic enzyme, bifunctional L(+)-tartrate dehydrogenase-D(+)-malate (decarboxylating). This enzyme participates in butanoate metabolism. Group: Enzymes. Synonyms: D-malate dehydrogenase; D-malic enzyme; bifunctional L(+)-tartrate dehydrogenase-D(+)-malate (decarboxylating). Enzyme Commission Number: EC 1.1.1.83. CAS No. 37250-20-7. D-MDH. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0367; D-malate dehydrogenase (decarboxylating); EC 1.1.1.83; 37250-20-7; D-malate dehydrogenase; D-malic enzyme; bifunctional L(+)-tartrate dehydrogenase-D(+)-malate (decarboxylating). Cat No: EXWM-0367. | |
| ent-copalyl diphosphate synthase | Part of a bifunctional enzyme involved in the biosynthesis of kaurene. See also EC 4.2.3.19 (ent-kaurene synthase). Group: Enzymes. Synonyms: ent-kaurene synthase A; ent-kaurene synthetase A; ent-CDP synthase; ent-copalyl-diphosphate lyase (decyclizing). Enzyme Commission Number: EC 5.5.1.13. CAS No. 9055-64-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5614; ent-copalyl diphosphate synthase; EC 5.5.1.13; 9055-64-5; ent-kaurene synthase A; ent-kaurene synthetase A; ent-CDP synthase; ent-copalyl-diphosphate lyase (decyclizing). Cat No: EXWM-5614. | |
| ent-kaurene synthase | Part of a bifunctional enzyme involved in the biosynthesis of ent-kaurene. See also EC 5.5.1.13 (ent-copalyl diphosphate synthase). Group: Enzymes. Synonyms: ent-kaurene synthase B; ent-kaurene synthetase B, ent-copalyl-diphosphate diphosphate-lyase (cyclizing). Enzyme Commission Number: EC 4.2.3.19. CAS No. 9055-64-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5175; ent-kaurene synthase; EC 4.2.3.19; 9055-64-5; ent-kaurene synthase B; ent-kaurene synthetase B, ent-copalyl-diphosphate diphosphate-lyase (cyclizing). Cat No: EXWM-5175. | |
| FAD reductase [NAD(P)H] | This enzyme, isolated from the bacterium Geobacillus thermodenitrificans, participates in the pathway of tryptophan degradation. The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and EC 1.14.14.8, anthranilate 3-monooxygenase (FAD). It can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. The enzyme has a slight preference for NADPH as acceptor. cf. EC 1.5.1.37, FAD reductase (NADH). Group: Enzymes. Synonyms: GTNG_3158 (gene name). Enzyme Commission Number: EC 1.5.1.45. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1526; FAD reductase [NAD(P)H]; EC 1.5.1.45; GTNG_3158 (gene name). Cat No: EXWM-1526. | |
| FAD synthetase | Requires Mg2+ and is highly specific for ATP as phosphate donor. The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates. While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26, riboflavin kinase. Group: Enzymes. Synonyms: FAD pyrophosphorylase; riboflavin mononucleotide adenylyltransferase; adenosine triphosphate-riboflavin mononucleotide transadenylase; adenosine triphosphate-riboflavine mononucleotide transadenylase; riboflavin adenine dinucleotide pyrophosp. Enzyme Commission Number: EC 2.7.7.2. CAS No. 9026-37-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3234; FAD synthetase; EC 2.7.7.2; 9026-37-3; FAD pyrophosphorylase; riboflavin mononucleotide adenylyltransferase; adenosine triphosphate-riboflavin mononucleotide transadenylase; adenosine triphosphate-riboflavine mononucleotide transadenylase; riboflavin adenine dinucleotide pyrophosphorylase; riboflavine adenine dinucleotide adenylyltransferase; flavin adenine dinucleotide synthetase; FADS; FMN adenylyltransferase. Cat No: EXWM-3234. | |
| formimidoyltetrahydrofolate cyclodeaminase | In eukaroytes, occurs as a bifunctional enzyme that also has glutamate formimidoyltransferase (EC 2.1.2.5) activity. Group: Enzymes. Synonyms: formiminotetrahydrofolate cyclodeaminase; 5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing). Enzyme Commission Number: EC 4.3.1.4. CAS No. 9032-5-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5292; formimidoyltetrahydrofolate cyclodeaminase; EC 4.3.1.4; 9032-05-7; formiminotetrahydrofolate cyclodeaminase; 5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing). Cat No: EXWM-5292. | |
| GDP-mannose 4,6-dehydratase | The bacterial enzyme requires bound NAD+. This enzyme forms the first step in the biosynthesis of GDP-α-D-rhamnose and GDP-β-L-fucose. In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalysing the above reaction as well as the reaction catalysed by EC 1.1.1.281, GDP-4-dehydro-6-deoxy-D-mannose reductase. Belongs to the short-chain dehydrogenase/reductase enzyme family, having homologous structures and a conserved catalytic triad of Lys, Tyr and Ser/Thr residues. Group: Enzymes. Synonyms: guanosine 5'-diphosphate-D-mannose oxidoreductase; guanosine diphosphomannose oxidoreductase; guanosine diphosphomannose 4,6-dehydratase; GDP-D-mannose dehydratase; GDP-D-mannose 4,6-dehydratase; Gmd; GDP-mannose 4,6-hydro-lyase; GDP-mannose 4,6-hydro-. Enzyme Commission Number: EC 4.2.1.47. CAS No. 37211-59-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5036; GDP-mannose 4,6-dehydratase; EC 4.2.1.47; 37211-59-9; guanosine 5'-diphosphate-D-mannose oxidoreductase; guanosine diphosphomannose oxidoreductase; guanosine diphosphomannose 4,6-dehydratase; GDP-D-mannose dehydratase; GDP-D-mannose 4,6-dehydratase; Gmd; GDP-mannose 4,6-hydro-lyase; GDP-mannose 4,6-hydro-lyase (GDP-4-dehydro-6-deoxy-D-mannose-forming). Cat No: EXWM-5036. | |
| geosmin synthase | Requires Mg2+. Geosmin is the cause of the characteristic smell of moist soil. It is a bifunctional enzyme. The N-terminal part of the enzyme is EC 4.2.3.22, germacradienol synthase, and forms germacradienol from FPP. The C-terminal part of the enzyme catalyses the conversion of germacradienol to geosmin via (1S,4aS,8aS)-1,4a-dimethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalene. Group: Enzymes. Enzyme Commission Number: EC 4.1.99.16. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4930; geosmin synthase; EC 4.1.99.16. Cat No: EXWM-4930. | |
| geraniol isomerase | In absence of oxygen the bifunctional linalool dehydratase-isomerase can catalyse in vitro two reactions, the isomerization of (3S)-linalool to geraniol and the hydration of myrcene to (3S)-linalool, the latter activity being classified as EC 4.2.1.127, linalool dehydratase. Group: Enzymes. Enzyme Commission Number: EC 5.4.4.4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5545; geraniol isomerase; EC 5.4.4.4. Cat No: EXWM-5545. | |
| GlcNAc-1-phosphate uridyltransferase from Campylobacter jejuni, Recombinant | N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme exclusive to prokaryotes, belongs to the family of sugar nucleotidyltransferases (SNTs). The enzyme binds GlcNAc-1-P and UTP, and catalyzes a uridyltransfer reaction to synthesize UDP-GlcNAc, an important precursor for cell-wall biosynthesis. Group: Enzymes. Synonyms: N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157. Enzyme Commission Number: EC 2.3.1.157. Purity: min 95% by SDS-PAGE. GlcNAc1-phosphate uridyltransferase. Source: E. coli. Species: Campylobacter jejuni. N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157; GlcNAc1-P Uridyltransferase. Cat No: NATE-1492. | |
| GlcNAc1-phosphate uridyltransferase from E. coli K-12, Recombinant | N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme exclusive to prokaryotes, belongs to the family of sugar nucleotidyltransferases (SNTs). The enzyme binds GlcNAc-1-P and UTP, and catalyzes a uridyltransfer reaction to synthesize UDP-GlcNAc, an important precursor for cell-wall biosynthesis. Group: Enzymes. Synonyms: N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157. Enzyme Commission Number: EC 2.3.1.157. Purity: min 95% by SDS-PAGE. GlcNAc1-phosphate uridyltransferase. Mole weight: 25 kDa. Source: E. coli. Species: E. coli K-12. N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157; GlcNAc1-P Uridyltransferase. Cat No: NATE-1482. | |
| GlcNAc-1-phosphate uridyltransferase from Human, Recombinant | N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme exclusive to prokaryotes, belongs to the family of sugar nucleotidyltransferases (SNTs). The enzyme binds GlcNAc-1-P and UTP, and catalyzes a uridyltransfer reaction to synthesize UDP-GlcNAc, an important precursor for cell-wall biosynthesis. Group: Enzymes. Synonyms: N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157. Enzyme Commission Number: EC 2.3.1.157. CAS No. 9023-06-7;9031-91-8. Purity: min 95% by SDS-PAGE. GlcNAc1-phosphate uridyltransferase. Source: E. coli. Species: Human. N-Acetylglucosamine-1-phosphate uridyltransferase; GlmU; EC 2.3.1.157; GlcNAc1-P Uridyltransferase. Cat No: NATE-1500. | |
| glucosamine-1-phosphate N-acetyltransferase | The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Hemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Group: Enzymes. Enzyme Commission Number: EC 2.3.1.157. CAS No. 9031-91-8. GlcNAc1-phosphate uridyltransferase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2096; glucosamine-1-phosphate N-acetyltransferase; EC 2.3.1.157; 9031-91-8. Cat No: EXWM-2096. | |
| glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase | Involved in the biosynthesis of chondroitin sulfate. The human form of this enzyme is a bifunctional glycosyltransferase, which also has the 3-β-glucuronosyltransferase (EC 2.4.1.226, N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase) activity required for the synthesis of the chondroitin sulfate disaccharide repeats. Similar chondroitin synthase 'co-polymerases' can be found in Pasteurella multocida and Escherichia coli. Group: Enzymes. Synonyms: N-acetylgalactosaminyltransferase II; UDP-N-acetyl-D-galactosamine:D-glucuronyl-N-acetyl-1,3-β-D-galactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; cho...curonosyl-N-acetylgalactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase; EC 2.4.1.175; 96189-40-1; N-acetylgalactosaminyltransferase II; UDP-N-acetyl-D-galactosamine:D-glucuronyl-N-acetyl-1,3-β-D-galactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; chondroitin synthase; glucuronyl-N-acetylgalactosaminylproteoglycan β-1,4-N-acetylgalactosaminyltransferase; uridine diphosphoacetylgalactosamine-chondroitin acetylgalactosaminyltransferase II; UDP-N-acetyl-D-galactosamine:β-D-glucuronosyl-(1?3)-N-acetyl-β-D-galactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase. Cat No: EXWM-2400. | |
| glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase | Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the enzyme from human (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the 4-β-glucuronosyltransferase (EC 2.4.1.225, N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase) activity required for the synthesis of the heparan sulfate disaccharide repeats. Other human forms of this enzyme (e.g. the product of the EXTL1 gene) have only the 4-α-N-acetylglucosaminyltransferase activity. In Caenorhabditis elegans, the product of the rib-2 gene displays the activities of this enzyme as well as EC 2.4.1.223, glucuronosyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase. Group: Enzymes. Synonyms: α-N-acetylglucosaminyltransferase II glucuronyl-. Enzyme Commission Number: EC 2.4.1.224. CAS No. 336193-98-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2453; glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase; EC 2.4.1.224; 336193-98-7; α-N-acetylglucosaminyltransferase II glucuronyl-N-acetylglucosaminylproteoglycan α-1,4-N-acetylglucosaminyltransferase. Cat No: EXWM-2453. | |
| glutamate formimidoyltransferase | A pyridoxal-phosphate protein. Also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate (a reaction formerly listed as EC 2.1.2.6). In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity. Group: Enzymes. Synonyms: glutamate formyltransferase; formiminoglutamic acid transferase; formiminoglutamic formiminotransferase; glutamate formiminotransferase. Enzyme Commission Number: EC 2.1.2.5. CAS No. 9032-83-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2007; glutamate formimidoyltransferase; EC 2.1.2.5; 9032-83-1; glutamate formyltransferase; formiminoglutamic acid transferase; formiminoglutamic formiminotransferase; glutamate formiminotransferase. Cat No: EXWM-2007. | |
| [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase | This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42, [glutamine synthetase] adenylyltransferase). The two activities are present on separate domains. Group: Enzymes. Synonyms: adenylyl-[glutamine-synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase. Enzyme Commission Number: EC 2.7.7.89. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3302; [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase; EC 2.7.7.89; adenylyl-[glutamine-synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase. Cat No: EXWM-3302. | |
| [glutamine synthetase] adenylyltransferase | This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also catalyses a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89, [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase). The two activities are present on separate domains. Group: Enzymes. Synonyms: glutamine-synthetase adenylyltransferase; ATP:glutamine synthetase adenylyltransferase; adenosine triphosphate:glutamine synthetase adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase; [glutamate-ammonia-ligase] adenylyltransferase. Enzyme Commission Number: EC 2.7.7.42. CAS No. 9077-66-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3254; [glutamine synthetase] adenylyltransferase; EC 2.7.7.42; 9077-66-1; glutamine-synthetase adenylyltransferase; ATP:glutamine synthetase adenylyltransferase; adenosine triphosphate:glutamine synthetase adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase; [glutamate-ammonia-ligase] adenylyltransferase. Cat No: EXWM-3254. | |
| glutathionylspermidine amidase | Spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP. Group: Enzymes. Synonyms: glutathionylspermidine amidohydrolase (spermidine-forming). Enzyme Commission Number: EC 3.5.1.78. CAS No. 171040-71-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4469; glutathionylspermidine amidase; EC 3.5.1.78; 171040-71-4; glutathionylspermidine amidohydrolase (spermidine-forming). Cat No: EXWM-4469. | |
| glutathionylspermidine synthase | Requires magnesium ions. Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78) reaction, resulting in a net hydrolysis of ATP. Group: Enzymes. Synonyms: glutathione:spermidine ligase (ADP-forming). Enzyme Commission Number: EC 6.3.1.8. CAS No. 9077-9-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5728; glutathionylspermidine synthase; EC 6.3.1.8; 9077-09-2; glutathione:spermidine ligase (ADP-forming). Cat No: EXWM-5728. | |
| glycerol-3-phosphate 2-O-acyltransferase | A membrane-associated enzyme required for suberin or cutin synthesis in plants. Active with a wide range of acyl-CoA substrates (C16:0-C24:0). The enzyme from some sources has much higher activity with ω-oxidized acyl-CoAs. Some enzymes are bifunctional and have an additional phosphatase activity producing sn-2-monoacylglycerols. Group: Enzymes. Synonyms: sn-2-glycerol-3-phosphate O-acyltransferase; glycerol-3-phosphate O-acyltransferase (ambiguous). Enzyme Commission Number: EC 2.3.1.198. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2141; glycerol-3-phosphate 2-O-acyltransferase; EC 2.3.1.198; sn-2-glycerol-3-phosphate O-acyltransferase; glycerol-3-phosphate O-acyltransferase (ambiguous). Cat No: EXWM-2141. | |
| GTP 3',8-cyclase | The enzyme catalyses an early step in the biosynthesis of the molybdenum cofactor (MoCo). In bacteria and plants the reaction is catalysed by MoaA and Cnx2, respectively. In mammals it is catalysed by the MOCS1A domain of the bifunctional MOCS1 protein, which also catalyses EC 4.6.1.17, cyclic pyranopterin monophosphate synthase. The enzyme belongs to the superfamily of radical S-adenosyl-L-methionine (radical SAM) enzymes, and contains two oxygen-sensitive FeS clusters. Group: Enzymes. Synonyms: MOCS1A (gene name); moaA (gene name); cnx2 (gene name). Enzyme Commission Number: EC 4.1.99.22. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4935; GTP 3',8-cyclase; EC 4.1.99.22; MOCS1A (gene name); moaA (gene name); cnx2 (gene name). Cat No: EXWM-4935. | |
| (Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase | The bifunctional enzyme from Escherichia coli transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf. EC 2.4.99.12 [lipid IVA 3-deoxy-D-manno-octulosonic acid transferase]). The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes. Group: Enzymes. Synonyms: Kdo transferase; waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; (KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase. Enzyme Commission Number: EC 2.4.99.13. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2697; (Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase; EC 2.4.99.13; Kdo transferase; waaA (gene name); kdtA (gene name); 3-deoxy-D-manno-oct-2-ulosonic acid transferase; 3-deoxy-manno-octulosonic acid transferase; (KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase. Cat No: EXWM-2697. | |
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