Find where to buy products from suppliers in the USA, including: distributors, industrial manufacturers in America, bulk supplies and wholesalers of raw ingredients & finished goods.
Search for products or services, then visit the American suppliers website for prices, SDS or more information. You can also view suppliers in Australia, NZ or the UK.
| Product | Description | |
|---|---|---|
| 15,16-dihydrobiliverdin:ferredoxin oxidoreductase | Catalyses the two-electron reduction of biliverdin IXα at the C15 methine bridge. It has been proposed that this enzyme and EC 1.3.7.3, phycoerythrobilin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXα into phycoerythrobilin. Group: Enzymes. Synonyms: PebA. Enzyme Commission Number: EC 1.3.7.2. CAS No. 347401-20-1. 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-1397; 15,16-dihydrobiliverdin:ferredoxin oxidoreductase; EC 1.3.7.2; 347401-20-1; PebA. Cat No: EXWM-1397. |  |
| 3,8-divinyl chlorophyllide a reductase | The enzyme, found only in bacteriochlorophyll b-producing bacteria, catalyses the introduction of a C-8 ethylidene group. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase. It is very similar to EC 1.3.7.15, chlorophyllide a reductase, and is composed of three subunits. Two of them form the catalytic component, while the third one functions as an ATP-dependent reductase component that catalyses the electron transfer from ferredoxin to the catalytic component. Group: Enzymes. Enzyme Commission Number: EC 1.3.7.14. 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-1395; 3,8-divinyl chlorophyllide a reductase; EC 1.3.7.14. Cat No: EXWM-1395. | |
| 4-(γ-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase | Catalyses a step in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. FMNH2 is used as a free cofactor. Forms a complex with a dedicated NAD(P)H:FMN oxidoreductase. The enzyme is not able to hydroxylate free substrates, activation by the acyl-carrier protein is mandatory.Octanoyl-S-[BtrI acyl-carrier protein] is also accepted. Group: Enzymes. Synonyms: btrO (gene name). Enzyme Commission Number: EC 1.14.14.13. 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-0910; 4-(γ-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase; EC 1.14.14.13; btrO (gene name). Cat No: EXWM-0910. | |
| 5,6-dimethylbenzimidazole synthase | The enzyme catalyses a complex oxygen-dependent conversion of reduced flavin mononucleotide to form 5,6-dimethylbenzimidazole, the lower ligand of vitamin B12. This conversion involves many sequential steps in two distinct stages, and an alloxan intermediate that acts as a proton donor, a proton acceptor, and a hydride acceptor. The C-2 of 5,6-dimethylbenzimidazole is derived from C-1' of the ribityl group of FMNH2 and 2-H from the ribityl 1'-pro-S hydrogen. While D-erythrose 4-phosphate has been shown to be one of the byproducts, the nature of the other product(s) has not been verified yet. Group: Enzymes. Synonyms: BluB. Enzyme Commission Number: EC 1.13.11.79. 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-0599; 5,6-dimethylbenzimidazole synthase; EC 1.13.11.79; BluB. Cat No: EXWM-0599. | |
| 5-methyltetrahydrosarcinapterin: corrinoid/iron-sulfur protein Co-methyltransferase | Catalyses the transfer of a methyl group from the cobamide cofactor of a corrinoid/Fe-S protein to the N5 group of tetrahydrosarcinapterin. Forms, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, the acetyl-CoA decarbonylase/synthase complex that catalyses the demethylation of acetyl-CoA in a reaction that also forms CO2. This reaction is a key step in methanogenesis from acetate. Group: Enzymes. Synonyms: cdhD (gene name); cdhE (gene name). Enzyme Commission Number: EC 2.1.1.245. 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-1848; 5-methyltetrahydrosarcinapterin: corrinoid/iron-sulfur protein Co-methyltransferase; EC 2.1.1.245; cdhD (gene name); cdhE (gene name). Cat No: EXWM-1848. | |
| acetoin dehydrogenase | Requires thiamine diphosphate. This enzyme, which belongs to the family of 2-oxo acid dehydrogenase complexes, catalyses the oxidative-hydrolytic cleavage of acetoin to acetaldehyde and acetyl-CoA in many bacterial strains, both aerobic and anaerobic. The enzyme is composed of multiple copies of three enzymic components: acetoin oxidoreductase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoyl dehydrogenase (E3). Group: Enzymes. Synonyms: acetoin dehydrogenase complex; acetoin dehydrogenase enzyme system; AoDH ES. Enzyme Commission Number: EC 2.3.1.190. 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-2133; acetoin dehydrogenase; EC 2.3.1.190; acetoin dehydrogenase complex; acetoin dehydrogenase enzyme system; AoDH ES. Cat No: EXWM-2133. | |
| acrylyl-CoA reductase (NADH) | Contains FAD. The reaction is catalysed in the opposite direction to that shown. The enzyme from the bacterium Clostridium propionicum is a complex that includes an electron-transfer flavoprotein (ETF). The ETF is reduced by NADH and transfers the electrons to the active site. Catalyses a step in a pathway for L-alanine fermentation to propanoate. cf. EC 1.3.1.84, acrylyl-CoA reductase (NADPH). Group: Enzymes. Enzyme Commission Number: EC 1.3.1.95. 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-1365; acrylyl-CoA reductase (NADH); EC 1.3.1.95. Cat No: EXWM-1365. | |
| ADP-thymidine kinase | The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyses this reaction as well as those of EC 2.7.1.21 (thymidine kinase), EC 2.7.1.114 (AMP-thymidine kinase) and EC 2.7.4.9 (dTMP kinase). Group: Enzymes. Synonyms: ADP:dThd phosphotransferase; adenosine diphosphate-thymidine phosphotransferase. Enzyme Commission Number: EC 2.7.1.118. CAS No. 82114-39-4. 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-2958; ADP-thymidine kinase; EC 2.7.1.118; 82114-39-4; ADP:dThd phosphotransferase; adenosine diphosphate-thymidine phosphotransferase. Cat No: EXWM-2958. | |
| AMP-thymidine kinase | The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyses this reaction as well as those of EC 2.7.1.21 (thymidine kinase), EC 2.7.1.118 (ADP-thymidine kinase) and EC 2.7.4.9 (dTMP kinase). Group: Enzymes. Synonyms: adenylate-nucleoside phosphotransferase. Enzyme Commission Number: EC 2.7.1.114. CAS No. 60440-28-0. 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-2957; AMP-thymidine kinase; EC 2.7.1.114; 60440-28-0; adenylate-nucleoside phosphotransferase. Cat No: EXWM-2957. | |
| anaerobic carbon-monoxide dehydrogenase | This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [...-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase. Group: Enzymes. Synonyms: Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Enzyme Commission Number: EC 1.2.7.4. 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-1227; anaerobic carbon-monoxide dehydrogenase; EC 1.2.7.4; Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Cat No: EXWM-1227. | |
| caldariellaquinol oxidase (H+-transporting) | A copper-containing cytochrome. The enzyme from thermophilic archaea is part of the terminal oxidase and catalyses the reduction of O2 to water, accompanied by the extrusion of protons across the cytoplasmic membrane. Group: Enzymes. Synonyms: SoxABCD quinol oxidase; SoxABCD complex; quinol oxidase SoxABCD; SoxM supercomplex; aa3-type quinol oxidase; aa3 quinol oxidase; cytochrome aa3; terminal quinol oxidase; terminal quinol:oxygen oxidoreductase; caldariella quinol:dioxygen oxidoreductase; cytochrome aa3-type oxidase caldariellaquinol:O2 oxidoreductase (H+-transporting). Enzyme Commission Number: EC 7.1.1.4 (Formerly EC 1.10.3.13). 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-0479; caldariellaquinol oxidase (H+-transporting); EC 1.10.3.13; SoxABCD quinol oxidase; SoxABCD complex; quinol oxidase SoxABCD; SoxM supercomplex; aa3-type quinol oxidase; aa3 quinol oxidase; cytochrome aa3; terminal quinol oxidase; terminal quinol:oxygen oxidoreductase; caldariella quinol:dioxygen oxidoreductase; cytochrome aa3-type oxidase caldariellaquinol:O2 oxidoreductase (H+-transporting). Cat No: EXWM-0479. | |
| carbazole 1,9a-dioxygenase | This enzyme catalyses the first reaction in the pathway of carbazole degradation. The enzyme attacks at the 1 and 9a positions of carbazole, resulting in the formation of a highly unstable hemiaminal intermediate that undergoes a spontaneous cleavage and rearomatization, resulting in 2'-aminobiphenyl-2,3-diol. In most bacteria the enzyme is a complex composed of a terminal oxygenase, a ferredoxin, and a ferredoxin reductase. The terminal oxygenase component contains a nonheme iron centre and a Rieske [2Fe-2S] iron-sulfur cluster. Group: Enzymes. Synonyms: CARDO. Enzyme Commission Number: EC 1.14.12.22. 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-0689; carbazole 1,9a-dioxygenase; EC 1.14.12.22; CARDO. Cat No: EXWM-0689. | |
| chlorophyllide-a oxygenase | Chlorophyll b is required for the assembly of stable light-harvesting complexes (LHCs) in the chloroplast of green algae, cyanobacteria and plants. Contains a mononuclear iron centre. The enzyme catalyses two successive hydroxylations at the 7-methyl group of chlorophyllide a. The second step yields the aldehyde hydrate, which loses H2O spontaneously to form chlorophyllide b. Chlorophyll a and protochlorophyllide a are not substrates. Group: Enzymes. Synonyms: chlorophyllide a oxygenase; chlorophyll-b synthase; CAO. Enzyme Commission Number: EC 1.14.13.122. CAS No. 216503-73-0. 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-0723; chlorophyllide-a oxygenase; EC 1.14.13.122; 216503-73-0; chlorophyllide a oxygenase; chlorophyll-b synthase; CAO. Cat No: EXWM-0723. | |
| chlorophyllide a reductase | The enzyme, together with EC 1.1.1.396, bacteriochlorophyllide-a dehydrogenase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. This enzyme catalyses a trans-reduction of the B-ring; the product has the (7R,8R)-configuration. In addition, the enzyme has a latent activity of EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin). The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction. Group: Enzymes. Synonyms: bchX (gene name); bchY (gene name); bchZ (gene name); COR. Enzyme Commission Number: EC 1.3.7.15. 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-1396; chlorophyllide a reductase; EC 1.3.7.15; bchX (gene name); bchY (gene name); bchZ (gene name); COR. Cat No: EXWM-1396. | |
| coenzyme-B sulfoethylthiotransferase | This enzyme catalyses the final step in methanogenesis, the biological production of methane. This important anaerobic process is carried out only by methanogenic archaea. The enzyme can also function in reverse, for anaerobic oxidation of methane.The enzyme requires the hydroporphinoid nickel complex coenzyme F430. Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates. The sulfide sulfur can be replaced by selenium but not by oxygen. Group: Enzymes. Synonyms: methyl-CoM reductase; methyl coenzyme M reductase. Enzyme Commission Number: EC 2.8.4.1. 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-3427; coenzyme-B sulfoethylthiotransferase; EC 2.8.4.1; methyl-CoM reductase; methyl coenzyme M reductase. Cat No: EXWM-3427. | |
| Diaphorase 22 from Recombinant E.coli | A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoami...(NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.8.1.4. CAS No. 9001-18-7. Diaphorase. Mole weight: ca. 110,000. Activity: >150 U/mg protein. Storage: Store at -20°C. Form: Lyophilized. Source: E. coli. LDP-Glc; LDP-Val; dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate d | |
| dichloroarcyriaflavin A synthase | The conversion of dichlorochromopyrrolate to dichloroarcyriaflavin A is a complex process that involves two enzyme components. RebP is an NAD-dependent cytochrome P-450 oxygenase that performs an aryl-aryl bond formation yielding the six-ring indolocarbazole scaffold. Along with RebC, a flavin-dependent hydroxylase, it also catalyses the oxidative decarboxylation of both carboxyl groups. The presence of RebC ensures that the only product is the rebeccamycin aglycone dichloroarcyriaflavin A. The enzymes are similar, but not identical, to StaP and StaC, which are involved in the synthesis of staurosporine. Group: Enzymes. Enzyme Commission Number: EC 1.13.12.17. 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-0609; dichloroarcyriaflavin A synthase; EC 1.13.12.17. Cat No: EXWM-0609. | |
| dihydrolipoyl dehydrogenase | A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or...tase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.8.1.4. CAS No. 9001-18-7. Diaphorase. 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-1648; dihydrolipoyl dehydrogenase; EC 1.8.1.4; 9001-18-7; LDP-Glc; LDP-Val; dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxido | |
| dTDP-4-dehydrorhamnose reductase | In the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase. Group: Enzymes. Synonyms: dTDP-4-keto-L-rhamnose reductase; dTDP-4-ketorhamnose reductase; TDP-4-keto-rhamnose reductase; thymidine diphospho-4-ketorhamnose reductase; dTDP-6-deoxy-L-mannose:NADP+ 4-oxidoreductase; dTDP-6-deoxy-β-L-mannose:NADP+ 4-oxidoreductase. Enzyme Commission Number: EC 1.1.1.133. CAS No. 37250-64-9. 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-0037; dTDP-4-dehydrorhamnose reductase; EC 1.1.1.133; 37250-64-9; dTDP-4-keto-L-rhamnose reductase; dTDP-4-ketorhamnose reductase; TDP-4-keto-rhamnose reductase; thymidine diphospho-4-ketorhamnose reductase; dTDP-6-deoxy-L-mannose:NADP+ 4-oxidoreductase; dTDP-6-deoxy-β-L-mannose:NADP+ 4-oxidoreductase. Cat No: EXWM-0037. | |
| enterobactin synthase | This enzyme complex catalyses the conversion of three molecules each of 2,3-dihydroxybenzoate and L-serine to form the siderophore enterobactin. In Escherichia coli the complex is formed by EntB (an aryl carrier protein that has to be activated by 4'-phosphopantetheine), EntD (a phosphopantetheinyl transferase that activates EntB), EntE (catalyses the ATP-dependent condensation of 2,3-dihydroxybenzoate and holo-EntB to form the covalently arylated form of EntB), and EntF (a four domain protein that catalyses the activation of L-serine by ATP, the condensation of the activated L-serine with the activated 2,3-dihydroxybenzoate, and the trimerization of three such moieties to a single enterobactin molecule). Group: Enzymes. Synonyms: N-(2,3-dihydroxybenzoyl)-serine synthetase; 2,3-dihydroxybenzoylserine synthetase; 2,3-dihydroxybenzoate-serine ligase. Enzyme Commission Number: EC 6.3.2.14. CAS No. 37318-63-1. 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-5735; enterobactin synthase; EC 6.3.2.14; 37318-63-1; N-(2,3-dihydroxybenzoyl)-serine synthetase; 2,3-dihydroxybenzoylserine synthetase; 2,3-dihydroxybenzoate-serine ligase. Cat No: EXWM-5735. | |
| fatty-acyl-CoA synthase | The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 2.3.1.41, 3-oxoacyl-[acyl-carrier-protein] synthase, while the other subunit catalyses the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 4.2.1.59, 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.1.1.279, (R)-3-hydroxyacid ester dehydrogenase. The enzyme differs from the animal enzyme (EC 2.3.1.85) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid. Group: Enzymes. Synonyms: yeast fatty acid synthase; FAS1 (gene name); FAS2 (gene name). Enzyme Commission Number: EC 2.3.1.86. CAS No. 94219-29-1. 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-2267; fatty-acyl-CoA synthase; EC 2.3.1.86; 94219-29-1; yeast fatty acid synthase; FAS1 (gene name); FAS2 (gene name). Cat No: EXWM-2267. | |
| ferredoxin:protochlorophyllide reductase (ATP-dependent) | Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction. Group: Enzymes. Synonyms: light-independent protochlorophyllide reductase. Enzyme Commission Number: EC 1.3.7.7. 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-1402; ferredoxin:protochlorophyllide reductase (ATP-dependent); EC 1.3.7.7; light-independent protochlorophyllide reductase. Cat No: EXWM-1402. | |
| ferric-chelate reductase (NADPH) | Contains FAD. The enzyme, which is widespread among bacteria, catalyses the reduction of ferric iron bound to a variety of iron chelators (siderophores), including ferric triscatecholates and ferric dicitrate, resulting in the release of ferrous iron. The enzyme from the bacterium Escherichia coli has the highest efficiency with the hydrolysed ferric enterobactin complex ferric N-(2,3-dihydroxybenzoyl)-L-serine. cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H]. Group: Enzymes. Synonyms: ferric chelate reductase (ambiguous); iron chelate reductase (ambiguous); NADPH:Fe3+-EDTA reductase; NADPH-dependent ferric reductase; yqjH (gene name); Fe(II):NADP+ oxidoreductase. Enzyme Commission Number: EC 1.16.1.9. CAS No. 120720-17-4. 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-1074; ferric-chelate reductase (NADPH); EC 1.16.1.9; 120720-17-4; ferric chelate reductase (ambiguous); iron chelate reductase (ambiguous); NADPH:Fe3+-EDTA reductase; NADPH-dependent ferric reductase; yqjH (gene name); Fe(II):NADP+ oxidoreductase. Cat No: EXWM-1074. | |
| glycosylceramidase | Broad specificity [cf. EC 3.2.1.45 (glucosylceramidase) and EC 3.2.1.46 (galactosylceramidase)]. Also hydrolyses phlorizin to phloretin and glucose. The intestinal enzyme is a complex that also catalyses the reaction of EC 3.2.1.108 lactase. Group: Enzymes. Synonyms: phlorizin hydrolase; phloretin-glucosidase; glycosyl ceramide glycosylhydrolase; cerebrosidase; phloridzin β-glucosidase; lactase-phlorizin hydrolase; phloridzin glucosidase. Enzyme Commission Number: EC 3.2.1.62. CAS No. 9033-10-7. 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-3926; glycosylceramidase; EC 3.2.1.62; 9033-10-7; phlorizin hydrolase; phloretin-glucosidase; glycosyl ceramide glycosylhydrolase; cerebrosidase; phloridzin β-glucosidase; lactase-phlorizin hydrolase; phloridzin glucosidase. Cat No: EXWM-3926. | |
| lactase | The enzyme from intestinal mucosa is isolated as a complex that also catalyses the reaction of EC 3.2.1.62 glycosylceramidase. cf. EC 3.2.1.33 amylo-α-1,6-glucosidase. Group: Enzymes. Synonyms: lactase-phlorizin hydrolase. Enzyme Commission Number: EC 3.2.1.108. CAS No. 9031-11-2. 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-3791; lactase; EC 3.2.1.108; 9031-11-2; lactase-phlorizin hydrolase. Cat No: EXWM-3791. | |
| lactose synthase | The enzyme is a complex of two proteins, A and B. In the absence of the B protein (α-lactalbumin), the enzyme catalyses the transfer of galactose from UDP-α-D-galactose to N-acetylglucosamine (EC 2.4.1.90 N-acetyllactosamine synthase). Group: Enzymes. Synonyms: UDP-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase. Enzyme Commission Number: EC 2.4.1.22. CAS No. 9030-11-9. Galactosyltransferase. 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-2448; lactose synthase; EC 2.4.1.22; 9030-11-9; UDP-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase. Cat No: EXWM-2448. | |
| long-chain acyl-protein thioester reductase | Together with a hydrolase component (EC 3.1.2.2 and EC 3.1.2.14) and a synthetase component (EC 6.2.1.19), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme is acylated by receiving an acyl group from EC 6.2.1.19, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA. Group: Enzymes. Synonyms: luxC (gene name); acyl-CoA reductase; acyl coenzyme A reductase; long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming); long-chain-fatty-acyl-CoA reductase. Enzyme Commission Number: EC 1.2.1.50. CAS No. 50936-56-6. 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-1154; long-chain acyl-protein thioester reductase; EC 1.2.1.50; 50936-56-6; luxC (gene name); acyl-CoA reductase; acyl coenzyme A reductase; long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming); long-chain-fatty-acyl-CoA reductase. Cat No: EXWM-1154. | |
| mRNA(cytosine6666) deaminase | The apolipoprotein B mRNA editing enzyme complex catalyses the editing of apolipoprotein B mRNA at cytidine6666 to uridine, thereby transforming the codon for glutamine-2153 to a termination codon. Editing results in translation of a truncated apolipoprotein B isoform (apoB-48) with distinct functions in lipid transport. The catalytic component (APOBEC-1) contains zinc at the active site. Group: Enzymes. Synonyms: APOBEC-1 (catalytic component of an RNA-editing complex); APOBEC1 (catalytic subunit); apolipoprotein B mRNA-editing enzyme 1 (catalytic component of an RNA-editing complex); apoB mRNA-editing enzyme catalytic polypeptide 1 (catalytic component of an RNA-editing complex); apoB mRNA editing complex; apolipoprotein B mRNA editing enzyme; REPR. Enzyme Commission Number: EC 3.5.4.36. 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-4564; mRNA(cytosine6666) deaminase; EC 3.5.4.36; APOBEC-1 (catalytic component of an RNA-editing complex); APOBEC1 (catalytic subunit); apolipoprotein B mRNA-editing enzyme 1 (catalytic component of an RNA-editing complex); apoB mRNA-editing enzyme catalytic polypeptide 1 (catalytic component of an RNA-editing complex); apoB mRNA editing complex; apolipoprotein B mRNA editing enzyme; REPR. Cat No: EXWM-4564. | |
| phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent) | Maximum activity is only obtained in the presence of α-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other α-D-hexoses, and the interconversion of α-D-ribose 1-phosphate and 5-phosphate. cf. EC 5.4.2.5, phosphoglucomutase (glucose-cofactor). Group: Enzymes. Synonyms: glucose phosphomutase; phosphoglucose mutase. Enzyme Commission Number: EC 5.4.2.2. CAS No. 9001-81-4. Phosphoglucomutase. 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-5524; phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent); EC 5.4.2.2; 9001-81-4; glucose phosphomutase; phosphoglucose mutase. Cat No: EXWM-5524. | |
| phosphonopyruvate decarboxylase | The enzyme catalyses a step in the biosynthetic pathway of 2-aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis. Requires thiamine diphosphate and Mg2+ as cofactors. The enzyme is activated by the divalent cations Mg2+, Ca2+ and Mn2+. Pyruvate and sulfopyruvate can also act as substrates, but more slowly. This enzyme drives the reaction catalysed by EC 5.4.2.9, phosphoenolpyruvate mutase, in the thermodynamically unfavourable direction of 3-phosphonopyruvate formation. It is the initial step in all of the major biosynthetic pathways of phosphonate natural products. Group: Enzymes. Synonyms: 3-phosphonopyruvate carboxy-lyase. Enzyme Commission Number: EC 4.1.1.82. CAS No. 151662-34-9. 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-4831; phosphonopyruvate decarboxylase; EC 4.1.1.82; 151662-34-9; 3-phosphonopyruvate carboxy-lyase. Cat No: EXWM-4831. | |
| phycoerythrobilin:ferredoxin oxidoreductase | Catalyses the two-electron reduction of the C2 and C31 diene system of 15,16-dihydrobiliverdin. Specific for 15,16-dihydrobiliverdin. It has been proposed that this enzyme and EC 1.3.7.2, 15,16-dihydrobiliverdin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXα to phycoerythrobilin. Group: Enzymes. Synonyms: PebB. Enzyme Commission Number: EC 1.3.7.3. CAS No. 347401-21-2. 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-1398; phycoerythrobilin:ferredoxin oxidoreductase; EC 1.3.7.3; 347401-21-2; PebB. Cat No: EXWM-1398. | |
| succinate dehydrogenase | A flavoprotein (FAD) complex containing iron-sulfur centres. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria and archaea. It catalyses succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II). In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone. cf. EC 1.3.5.4, fumarate reductase (quinone). Group: Enzymes. Synonyms: succinate dehydrogenase (quinone); succinate dehydrogenase (ubiquinone); succinic dehydrogenase; complex II (ambiguous); succinate dehydrogenase complex; SDH; succinate:ubiquinone oxidoreductase. Enzyme Commission Number: EC 1.3.5.1. CAS No. 9028-11-9. 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-1385; succinate dehydrogenase; EC 1.3.5.1; 9028-11-9; succinate dehydrogenase (quinone); succinate dehydrogenase (ubiquinone); succinic dehydrogenase; complex II (ambiguous); succinate dehydrogenase complex; SDH; succinate:ubiquinone oxidoreductase. Cat No: EXWM-1385. | |
| thymidine kinase | Deoxyuridine can also act as acceptor, and dGTP can act as a donor. The deoxypyrimidine kinase complex induced by Herpes simplex virus catalyses this reaction as well as those of EC 2.7.1.114 (AMP-thymidine kinase), EC 2.7.1.118 (ADP-thymidine kinase) and EC 2.7.4.9 (dTMP-kinase). Group: Enzymes. Synonyms: thymidine kinase (phosphorylating); 2'-deoxythymidine kinase; deoxythymidine kinase (phosphorylating). Enzyme Commission Number: EC 2.7.1.21. CAS No. 9002-6-6. HSV-1 TK. 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-3045; thymidine kinase; EC 2.7.1.21; 9002-06-6; thymidine kinase (phosphorylating); 2'-deoxythymidine kinase; deoxythymidine kinase (phosphorylating). Cat No: EXWM-3045. | |
| acetyl-S-ACP:malonate ACP transferase | This is the first step in the catalysis of malonate decarboxylation and involves the exchange of an acetyl thioester residue bound to the activated acyl-carrier protein (ACP) subunit of the malonate decarboxylase complex for a malonyl thioester residue. This enzyme forms the α subunit of the multienzyme complexes biotin-independent malonate decarboxylase (EC 4.1.1.88) and biotin-dependent malonate decarboxylase (EC 4.1.1.89). The enzyme can also use acetyl-CoA as a substrate but more slowly. Group: Enzymes. Synonyms: acetyl-S-ACP:malonate ACP-SH transferase; acetyl-S-acyl-carrier protein:malonate acyl-carrier-protein-transferase; MdcA; MadA; ACP transferase; malonate/acetyl-CoA transferase; malonate:ACP transferase; acetyl-S-acyl carrier protein:malonate acyl carrier protein-SH transferase. Enzyme Commission Number: EC 2.3.1.187. 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-2129; acetyl-S-ACP:malonate ACP transferase; EC 2.3.1.187; acetyl-S-ACP:malonate ACP-SH transferase; acetyl-S-acyl-carrier protein:malonate acyl-carrier-protein-transferase; MdcA; MadA; ACP transferase; malonate/acetyl-CoA transferase; malonate:ACP transferase; acetyl-S-acyl carrier protein:malonate acyl carrier protein-SH transferase. Cat No: EXWM-2129. | |
| dihydrolipoyllysine-residue (2-methylpropanoyl)transferase | A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalysed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine. Group: Enzymes. Synonyms: dihydrolipoyl transacylase; enzyme-dihydrolipo. Enzyme Commission Number: EC 2.3.1.168. CAS No. 102784-26-9. 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-2108; dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; EC 2.3.1.168; 102784-26-9; dihydrolipoyl transacylase; enzyme-dihydrolipoyllysine:2-methylpropanoyl-CoA S-(2-methylpropanoyl)transferase; 2-methylpropanoyl-CoA:enzyme-6-N-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase. Cat No: EXWM-2108. | |
| dihydrolipoyllysine-residue acetyltransferase | A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalysed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A. Group: Enzymes. Synonyms: acetyl-CoA:dihydrolipoamide S-acetyltransferase; dihydrolipoamide S-acetyltransferase; d. Enzyme Commission Number: EC 2.3.1.12. CAS No. 9032-29-5. 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-2058; dihydrolipoyllysine-residue acetyltransferase; EC 2.3.1.12; 9032-29-5; acetyl-CoA:dihydrolipoamide S-acetyltransferase; dihydrolipoamide S-acetyltransferase; dihydrolipoate acetyltransferase; dihydrolipoic transacetylase; dihydrolipoyl acetyltransferase; lipoate acetyltransferase; lipoate transacetylase; lipoic acetyltransferase; lipoic acid acetyltransferase; lipoic transacetylase; lipoylacetyltransferase; thioltransacetylase A; transacetylase X; enzyme-dihydrolipoyllysine:acetyl-CoA S-acetyltransferase; acetyl-CoA:enzyme 6-N-(dihydrolipoyl)lysine S-acetyltransferase. Cat No: EXWM-2058. | |
| dihydrolipoyllysine-residue succinyltransferase | A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalysed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A. Group: Enzymes. Synonyms: dihydrolipoamide S-succinyltransferase; dihydrolipoamide succinyltransferase; dihydrolipoic transsuccinylase; dihydrolipolyl transsuccinylase; dihydrolipoyl transsuccinylase; lipoate succinyltrans. Enzyme Commission Number: EC 2.3.1.61. CAS No. 9032-28-4. 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-2241; dihydrolipoyllysine-residue succinyltransferase; EC 2.3.1.61; 9032-28-4; dihydrolipoamide S-succinyltransferase; dihydrolipoamide succinyltransferase; dihydrolipoic transsuccinylase; dihydrolipolyl transsuccinylase; dihydrolipoyl transsuccinylase; lipoate succinyltransferase (Escherichia coli); lipoic transsuccinylase; lipoyl transsuccinylase; succinyl-CoA:dihydrolipoamide S-succinyltransferase; succinyl-CoA:dihydrolipoate S-succinyltransferase; enzyme-dihydrolipoyllysine:succinyl-CoA S-succinyltransferase. Cat No: EXWM-2241. | |
| (methyl)glyoxal oxidase | The enzyme, originally characterized from the white rot fungus Phanerochaete chrysosporium, utilizes a free radical-coupled copper complex for catalysis. Group: Enzymes. Synonyms: glx1 (gene name); glx2 (gene name). Enzyme Commission Number: EC 1.2.3.15. 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-1209; (methyl)glyoxal oxidase; EC 1.2.3.15; glx1 (gene name); glx2 (gene name). Cat No: EXWM-1209. | |
| Nitrilase, Recombinant | Nitrilase enzymes catalyse the hydrolysis of nitriles to carboxylic acids and ammonia, without the formation of "free" amide intermediates. Nitrilases are involved in natural product biosynthesis and post translational modifications in plants, animals, fungi and certain prokaryotes. Nitrilases can also be used as catalysts in preparative organic chemistry. Among others, nitrilases have been used for the resolution of racemic mixtures. The isoelectric point (pi) of this protein is 8.1. native page analysis indicates that the active complex of this enzyme consists of 14 identical subunits. Group: Enzymes. Synonyms: nitrilase; acetonitrilase; benzonitrilase; EC 3.5.5.1; 9024-90-2. Enzyme Commission Number: EC 3.5.5.1. CAS No. 9024-90-2. Nitrilase. Mole weight: mol wt 41 kDa. Activity: > 2.0 units/mg. Storage: 2-8°C. Source: E. coli. nitrilase; acetonitrilase; benzonitrilase; EC 3.5.5.1; 9024-90-2. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0487. | |
| proteasome endopeptidase complex | A 20-S protein composed of 28 subunits arranged in four rings of seven. The outer rings are composed of α subunits, but the β subunits forming the inner rings are responsible for peptidase activity. In eukaryotic organisms there are up to seven different types of β subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities. The molecule is barrel-shaped, and the active sites are on the inner surfaces. Terminal apertures restrict access of substrates to the active sites. There is evidence that catalytic subunits are replaced by others under some conditions so as to alter the spec...atalytic proteinase; proteasome organelle; alkaline protease; 26S protease; tricorn proteinase; tricorn protease. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. 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-4374; proteasome endopeptidase complex; EC 3.4.25.1; 140879-24-9; ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; tricorn proteinase; tricorn protease. Cat No: EXWM-4374. | |
| protein-synthesizing GTPase | This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1α (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1α catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs. Group: Enzymes. Synonyms: elongation factor (EF); initiation factor (IF); peptide-release or termination factor. Enzyme Commission Number: EC 3.6.5.3. 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-4714; protein-synthesizing GTPase; EC 3.6.5.3; elongation factor (EF); initiation factor (IF); peptide-release or termination factor. Cat No: EXWM-4714. | |
| tRNA (guanine10-N2)-methyltransferase | In contrast to the archaeal enzyme tRNA (guanine10-N2)-dimethyltransferase (EC 2.1.1.213), tRNA (guanine10-N2)-methyltransferase from yeast does not catalyse the methylation from N2-methylguanine10 to N2-dimethylguanine10 in tRNA. Group: Enzymes. Synonyms: (m2G10) methyltransferase; Trm11-Trm112 complex. Enzyme Commission Number: EC 2.1.1.214. 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-1816; tRNA (guanine10-N2)-methyltransferase; EC 2.1.1.214; (m2G10) methyltransferase; Trm11-Trm112 complex. Cat No: EXWM-1816. | |
| UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase | This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function. Group: Enzymes. Synonyms: WlbA; WbpB. Enzyme Commission Number: EC 1.1.1.335. 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-0249; UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase; EC 1.1.1.335; WlbA; WbpB. Cat No: EXWM-0249. | |
Our database is helping our users find suppliers everyday.
