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| Product | Description | |
|---|---|---|
| Glycogen branching enzyme from Escherichia coli, Recombinant | Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a storage form of glucose. More specifically, during glycogen synthesis, a glucose 1-phosphate molecule reacts with uridine triphosphate (UTP) to become UDP-glucose, an activated form of glucose. The activated glucosyl unit of UDP-glucose is then transferred to the hydroxyl group at the C-4 of a terminal residue of glycogen to form an α-1,4-glycosidic linkage, a reaction catalyzed by glycogen synthase. Importantly, glycogen synthase can only catalyze the synthesis of α-1,4-glycosidic linkages. Since glycogen is a readily mobili...;-1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase. Enzyme Commission Number: EC 2.4.1.18. CAS No. 9001-97-2. Purity: > 95 % as judged by SDS-PAGE. Glycogen branching enzyme. Mole weight: 88157.0 Da. Activity: 15.44 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. Branching enzyme, amylo-(1,4?1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzymatic branching factor; branching glycosyltransferase; enzyme Q; glucos |  |
| 1-deoxy-D-xylulose-5-phosphate reductoisomerase | The enzyme requires Mn2+, Co2+ or Mg2+ for activity, with the first being most effective. The enzyme from several eubacteria, including Escherichia coli, forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here). The mechanism has been shown to be a retroaldol/aldol reaction. Group: Enzymes. Synonyms: DXP-reductoisomerase; 1-deoxy-D-xylulose-5-phosphate isomeroreductase; 2-C-methyl-D-erythritol 4-phosphate (MEP) synthase. Enzyme Commission Number: EC 1.1.1.267. CAS No. 210756-42-6. 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-0173; 1-deoxy-D-xylulose-5-phosphate reductoisomerase; EC 1.1.1.267; 210756-42-6; DXP-reductoisomerase; 1-deoxy-D-xylulose-5-phosphate isomeroreductase; 2-C-methyl-D-erythritol 4-phosphate (MEP) synthase. Cat No: EXWM-0173. | |
| 1-[N-[N-(2-Aminobenzoyl)glycyl]-4-nitro-L-phenylalanyl]-L-proline | It is a substrate for the fluorescent assay of angiotensin I-converting enzyme and of the bacterial dipeptidyl carboxypeptidase from Escherichia coli. Synonyms: 2-Aminobenzoylglycyl-4-nitrophenylalanyl-proline; Abz-Gly-p-nitro-Phe-Pro-OH; L-Proline,N-(2-aminobenzoyl)glycyl-4-nitro-L-phenylalanyl-; o-Aminobenzoylglycyl-p-nitro-L-phenylalanyl-L-proline. CAS No. 67482-93-3. Molecular formula: C23H25N5O7. Mole weight: 483.47. |  |
| 23S rRNA (adenine2503-C2)-methyltransferase | Contains an [4Fe-4S] cluster. This enzyme is a member of the 'AdoMet radical' (radical SAM) family. S-Adenosyl-L-methionine acts as both a radical generator and as the source of the appended methyl group. RlmN first transfers an CH2 group to a conserved cysteine (Cys355 in Escherichia coli), the generated radical from a second S-adenosyl-L-methionine then attacks the methyl group, exctracting a hydrogen. The formed radical forms a covalent intermediate with the adenine group of the tRNA. RlmN is an endogenous enzyme used by the cell to refine functions of the ribosome in protein synthesis. The enzyme methylates adenosine by a radical mechanism with CH2 from the S-adenosyl-L-methionine and retention of the hydrogen at C-2 of adenosine2503 of 23S rRNA. It will also methylate 8-methyladenosine2503 of 23S rRNA. cf. EC 2.1.1.224 [23S rRNA (adenine2503-C8)-methyltransferase]. Group: Enzymes. Synonyms: RlmN; YfgB; Cfr. Enzyme Commission Number: EC 2.1.1.192. 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-1792; 23S rRNA (adenine2503-C2)-methyltransferase; EC 2.1.1.192; RlmN; YfgB; Cfr. Cat No: EXWM-1792. | |
| 23S rRNA (guanine2069-N7)-methyltransferase | The enzyme specifically methylates guanine2069 at position N7 in 23S rRNA. In γ-proteobacteria the enzyme also catalyses EC 2.1.1.173, 23S rRNA (guanine2445-N2)-methyltransferase, while in β-proteobacteria the activities are carried out by separate proteins. The enzyme from the γ-proteobacterium Escherichia coli has RNA unwinding activity as well. Group: Enzymes. Synonyms: rlmK (gene name); 23S rRNA m7G2069 methyltransferase. Enzyme Commission Number: EC 2.1.1.264. 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-1869; 23S rRNA (guanine2069-N7)-methyltransferase; EC 2.1.1.264; rlmK (gene name); 23S rRNA m7G2069 methyltransferase. Cat No: EXWM-1869. | |
| 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | The enzyme from Escherichia coli requires Mg2+ or Mn2+. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here). Group: Enzymes. Synonyms: MECDP-synthase; 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol CMP-lyase (cyclizing). Enzyme Commission Number: EC 4.6.1.12. CAS No. 287480-92-6. 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-5349; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; EC 4.6.1.12; 287480-92-6; MECDP-synthase; 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol CMP-lyase (cyclizing). Cat No: EXWM-5349. | |
| 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase | The enzyme from Escherichia coli requires Mg2+ or Mn2+. ATP or UTP can replace CTP, but both are less effective. GTP and TTP are not substrates. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here). Group: Enzymes. Synonyms: MEP cytidylyltransferase. Enzyme Commission Number: EC 2.7.7.60. CAS No. 251990-59-7. 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-3272; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; EC 2.7.7.60; 251990-59-7; MEP cytidylyltransferase. Cat No: EXWM-3272. | |
| 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase | The enzyme from Pseudomonas acts equally well on NAD+ or NADP+, while that from Erwinia chrysanthemi and Escherichia coli is more specific for NAD+. Group: Enzymes. Synonyms: 2-keto-3-deoxygluconate 5-dehydrogenase; 2-keto-3-deoxy-D-gluconate dehydrogenase; 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic acid) dehydrogenase. Enzyme Commission Number: EC 1.1.1.127. CAS No. 37250-56-9. 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-0031; 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase; EC 1.1.1.127; 37250-56-9; 2-keto-3-deoxygluconate 5-dehydrogenase; 2-keto-3-deoxy-D-gluconate dehydrogenase; 2-keto-3-deoxygluconate (nicotinamide adenine dinucleotide (phosphate)) dehydrogenase; 2-keto-3-deoxy-D-gluconate (3-deoxy-D-glycero-2,5-hexodiulosonic acid) dehydrogenase. Cat No: EXWM-0031. | |
| 2-dehydropantolactone reductase (Re-specific) | The yeast enzyme differs from that from Escherichia coli [EC 1.1.1.214 2-dehydropantolactone reductase (Si-specific)], which is specific for the Si-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase. Group: Enzymes. Synonyms: 2-oxopantoyl lactone reductase; ketopantoyl lactone reductase; 2-ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (A-specific); (R)-pantolactone:NADP+ oxidoreductase (A-specific); 2-dehydropantolactone reductase (A-specific). Enzyme Commission Number: EC 1.1.1.168. CAS No. 37211-75-9. 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-0071; 2-dehydropantolactone reductase (Re-specific); EC 1.1.1.168; 37211-75-9; 2-oxopantoyl lactone reductase; ketopantoyl lactone reductase; 2-ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (A-specific); (R)-pantolactone:NADP+ oxidoreductase (A-specific); 2-dehydropantolactone reductase (A-specific). Cat No: EXWM-0071. | |
| 2-dehydropantolactone reductase (Si-specific) | The Escherichia coli enzyme differs from that from yeast [EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific)], which is specific for the Re-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase. Group: Enzymes. Synonyms: 2-oxopantoyl lactone reductase; 2-ketopantoyl lactone reductase; ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (B-specific); (R)-pantolactone:NADP+ oxidoreductase (B-specific); 2-dehydropantolactone reductase (B-specific). Enzyme Commission Number: EC 1.1.1.214. CAS No. 37211-75-9. 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-0119; 2-dehydropantolactone reductase (Si-specific); EC 1.1.1.214; 37211-75-9; 2-oxopantoyl lactone reductase; 2-ketopantoyl lactone reductase; ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (B-specific); (R)-pantolactone:NADP+ oxidoreductase (B-specific); 2-dehydropantolactone reductase (B-specific). Cat No: EXWM-0119. | |
| 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. | |
| 2-oxoglutarate reductase | The enzyme catalyses a reversible reaction. The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. The SerA enzyme from the bacterium Escherichia coli can also accept (S)-2-hydroxyglutarate with a much higher Km, and also catalyses the activity of EC 1.1.1.95, phosphoglycerate dehydrogenase. Group: Enzymes. Synonyms: serA (gene name). Enzyme Commission Number: EC 1.1.1.399. 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-0319; 2-oxoglutarate reductase; EC 1.1.1.399; serA (gene name). Cat No: EXWM-0319. | |
| 3-demethylubiquinol 3-O-methyltransferase | 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, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast.The enzymes from yeast, Escherichia coli and rat also catalyse the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate (a reac...COQ3 (gene name); Coq3 O-methyltransferase; ubiG (gene name, ambiguous). Enzyme Commission Number: EC 2.1.1.64. CAS No. 63774-48-1. 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-1966; 3-demethylubiquinol 3-O-methyltransferase; EC 2.1.1.64; 63774-48-1; 5-demethylubiquinone-9 methyltransferase; OMHMB-methyltransferase; 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase; S-adenosyl-L-methionine:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone-O-methyltransferase; COQ3 (gene name); Coq3 O-methyltransferase; ubiG (gene name, ambiguous). Cat No: EXWM-1966. | |
| 3-deoxy-2-octulosonidase | The enzyme from a bacteriophage catalyses the depolymerization of capsular polysaccharides containing 3-deoxy-2-octulosonide in the cell wall of Escherichia coli. Group: Enzymes. Synonyms: 2-keto-3-deoxyoctonate hydrolase; octulosylono hydrolase; octulofuranosylono hydrolase; octulopyranosylonohydrolase. Enzyme Commission Number: EC 3.2.1.124. CAS No. 103171-48-8. 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-3807; 3-deoxy-2-octulosonidase; EC 3.2.1.124; 103171-48-8; 2-keto-3-deoxyoctonate hydrolase; octulosylono hydrolase; octulofuranosylono hydrolase; octulopyranosylonohydrolase. Cat No: EXWM-3807. | |
| 3-deoxyoctulosonase | Releases Kdo (α- and β-linked 3-deoxy-D-manno-octulosonic acid) from different lipopolysaccharides, including Re-LPS from Escherichia coli and Salmonella, Rd-LPS from S. minnesota, and de-O-acyl-re-LPS. 4-Methylumbelliferyl-α-Kdo (α-Kdo-OMec) is also a substrate. Group: Enzymes. Synonyms: α-Kdo-ase. Enzyme Commission Number: EC 3.2.1.144. CAS No. 199128-67-1. 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-3827; 3-deoxyoctulosonase; EC 3.2.1.144; 199128-67-1; α-Kdo-ase. Cat No: EXWM-3827. | |
| 3-hydroxy acid dehydrogenase | The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids. The highest activity is seen with L-allo-threonine and D-threonine. The enzyme from Escherichia coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2-methylpropanoate. The enzyme has no activity with NAD+ or L-threonine (cf. EC 1.1.1.103, L-threonine 3-dehydrogenase). Group: Enzymes. Synonyms: ydfG (gene name); YMR226c (gene name). Enzyme Commission Number: EC 1.1.1.381. 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-0300; 3-hydroxy acid dehydrogenase; EC 1.1.1.381; ydfG (gene name); YMR226c (gene name). Cat No: EXWM-0300. | |
| 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. | |
| 3-oxo-5,6-didehydrosuberyl-CoA thiolase | The enzyme acts in the opposite direction. The enzymes from the bacteria Escherichia coli and Pseudomonas sp. Y2 also have the activity of EC 2.3.1.174 (3-oxoadipyl-CoA thiolase). Group: Enzymes. Synonyms: paaJ (gene name). Enzyme Commission Number: EC 2.3.1.223. 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-2170; 3-oxo-5,6-didehydrosuberyl-CoA thiolase; EC 2.3.1.223; paaJ (gene name). Cat No: EXWM-2170. | |
| 3-oxoadipyl-CoA thiolase | The enzyme from the bacterium Escherichia coli also has the activity of EC 2.3.1.223 (3-oxo-5,6-dehydrosuberyl-CoA thiolase). Group: Enzymes. Enzyme Commission Number: EC 2.3.1.174. CAS No. 403496-07-1. 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-2115; 3-oxoadipyl-CoA thiolase; EC 2.3.1.174; 403496-07-1. Cat No: EXWM-2115. | |
| 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase | The enzyme from Escherichia coli requires Mg2+ or Mn2+. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here). Group: Enzymes. Synonyms: CDP-ME kinase. Enzyme Commission Number: EC 2.7.1.148. CAS No. 263016-77-9. 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-2978; 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase; EC 2.7.1.148; 263016-77-9; CDP-ME kinase. Cat No: EXWM-2978. | |
| 4-hydroxy-2-oxoheptanedioate aldolase | Requires Co2+ or Mn2+ for activity. The enzyme is also able to catalyse the aldol cleavage of 4-hydroxy-2-oxopentanoate and 4-hydroxy-2-oxohexanoate, and can use 2-oxobutanoate as carbonyl donor, with lower efficiency. In the reverse direction, is able to condense a range of aldehyde acceptors with pyruvate. The enzyme from the bacterium Escherichia coli produces a racemic mixture of (4R)- and (4S)-hydroxy-2-oxoheptanedioate. Group: Enzymes. Synonyms: 2,4-dihydroxyhept-2-enedioate aldolase; HHED aldolase; 4-hydroxy-2-ketoheptanedioate aldolase; HKHD aldolase; HpcH; HpaI; 4-hydroxy-2-oxoheptanedioate succinate semialdehyde lyase (pyruvate-forming). Enzyme Commission Number: EC 4.1.2.52. 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-4889; 4-hydroxy-2-oxoheptanedioate aldolase; EC 4.1.2.52; 2,4-dihydroxyhept-2-enedioate aldolase; HHED aldolase; 4-hydroxy-2-ketoheptanedioate aldolase; HKHD aldolase; HpcH; HpaI; 4-hydroxy-2-oxoheptanedioate succinate semialdehyde lyase (pyruvate-forming). Cat No: EXWM-4889. | |
| 4-hydroxyphenylacetate 3-monooxygenase | The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds. The enzyme uses FADH2 as a substrate rather than a cofactor. FADH2 is provided by EC 1.5.1.36, flavin reductase (NADH). Group: Enzymes. Synonyms: p-hydroxyphenylacetate 3-hydroxylase; 4-hydroxyphenylacetic acid-3-hydroxylase; p-hydroxyphenylacetate hydroxylase (FAD); 4 HPA 3-hydroxylase; p-hydroxyphenylacetate 3-hydroxylase (FAD); HpaB. Enzyme Commission Number: EC 1.14.14.9. CAS No. 37256-71-6. 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-0933; 4-hydroxyphenylacetate 3-monooxygenase; EC 1.14.14.9; 37256-71-6; p-hydroxyphenylacetate 3-hydroxylase; 4-hydroxyphenylacetic acid-3-hydroxylase; p-hydroxyphenylacetate hydroxylase (FAD); 4 HPA 3-hydroxylase; p-hydroxyphenylacetate 3-hydroxylase (FAD); HpaB. Cat No: EXWM-0933. | |
| 4-hydroxy-tetrahydrodipicolinate reductase | Studies of the enzyme from the bacterium Escherichia coli have shown that the enzyme accepts (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate and not (S)-2,3-dihydrodipicolinate as originally thought. Group: Enzymes. Synonyms: dihydrodipicolinate reductase (incorrect); dihydrodipicolinic acid reductase (incorrect); 2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase (incorrect); dapB (gene name). Enzyme Commission Number: EC 1.17.1.8. 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-1084; 4-hydroxy-tetrahydrodipicolinate reductase; EC 1.17.1.8; dihydrodipicolinate reductase (incorrect); dihydrodipicolinic acid reductase (incorrect); 2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase (incorrect); dapB (gene name). Cat No: EXWM-1084. | |
| 4-hydroxy-tetrahydrodipicolinate synthase | Studies of the enzyme from the bacterium Escherichia coli have shown that the reaction can be divided into three consecutive steps: Schiff base formation between pyruvate and an active-site lysine, the addition of L-aspartate-semialdehyde, and finally transimination leading to cyclization with simultaneous dissociation of the product. Group: Enzymes. Synonyms: dihydrodipicolinate synthase (incorrect); dihydropicolinate synthetase (incorrect); dihydrodipicolinic acid synthase (incorrect); L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing); dapA (gene name). Enzyme Commission Number: EC 4.3.3.7. 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-5308; 4-hydroxy-tetrahydrodipicolinate synthase; EC 4.3.3.7; dihydrodipicolinate synthase (incorrect); dihydropicolinate synthetase (incorrect); dihydrodipicolinic acid synthase (incorrect); L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing); dapA (gene name). Cat No: EXWM-5308. | |
| (4S)-4-hydroxy-2-oxoglutarate aldolase | The enzyme from the bacterium Escherichia coli is specific for the (S) enantiomer. That enzyme is trifunctional, and also catalyses the reactions of EC 4.1.1.3, oxaloacetate decarboxylase and EC 4.1.2.14, 2-dehydro-3-deoxy-phosphogluconate aldolase. cf. EC 4.1.3.16, 4-hydroxy-2-oxoglutarate aldolase. Group: Enzymes. Synonyms: 2-oxo-4-hydroxyglutarate aldolase (ambiguous); hydroxyketoglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutaric aldolase (ambiguous); 2-keto-4-hydroxyglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutarate aldolase (ambiguous); 2-keto-4-hydroxyglutarate aldolase. Enzyme Commission Number: EC 4.1.3.42. CAS No. 9030-81-3. 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-4919; (4S)-4-hydroxy-2-oxoglutarate aldolase; EC 4.1.3.42; 9030-81-3; 2-oxo-4-hydroxyglutarate aldolase (ambiguous); hydroxyketoglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutaric aldolase (ambiguous); 2-keto-4-hydroxyglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutarate aldolase (ambiguous); 2-keto-4-hydroxyglutarate aldolase (ambiguous); 2-oxo-4-hydroxyglutaric aldolase (ambiguous); hydroxyketoglutarate aldolase (ambiguous); 2-keto-4-hydroxybutyrate aldolase (ambiguous); 4-hydroxy-2-oxoglutarate glyoxylate-lyase (ambiguous); eda (gene name). Cat No: EXWM-4919. | |
| 50S ribosomal protein L16 3-hydroxylase | The enzyme, characterized from the bacterium Escherichia coli, hydroxylates an arginine residue on the 50S ribosomal protein L16, and is involved in regulation of bacterial ribosome assembly. Group: Enzymes. Synonyms: ycfD (gene name). Enzyme Commission Number: EC 1.14.11.47. 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-0666; 50S ribosomal protein L16 3-hydroxylase; EC 1.14.11.47; ycfD (gene name). Cat No: EXWM-0666. | |
| 5'-deoxynucleotidase | The enzyme, characterized from the bacterium Escherichia coli, shows strict specificity towards deoxyribonucleoside 5'-monophosphates and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates. A divalent metal cation is required for activity, with cobalt providing the highest activity. Group: Enzymes. Synonyms: yfbR (gene name). Enzyme Commission Number: EC 3.1.3.89. 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-3695; 5'-deoxynucleotidase; EC 3.1.3.89; yfbR (gene name). Cat No: EXWM-3695. | |
| 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase | Requires phosphate and contains zinc. The enzyme from Escherichia coli also requires a reducing system. Unlike EC 2.1.1.13, methionine synthase, this enzyme does not contain cobalamin. Group: Enzymes. Synonyms: tetrahydropteroyltriglutamate methyltransferase; homocysteine methylase; methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase; methyl tetrahydropteroylpolyglutamate: homocysteine methyltransferase; cobalamin-independent methionine synthase; methionine synthase (cobalamin-independent); MetE. Enzyme Commission Number: EC 2.1.1.14. CAS No. 9068-29-5. 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-1735; 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase; EC 2.1.1.14; 9068-29-5; tetrahydropteroyltriglutamate methyltransferase; homocysteine methylase; methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase; methyl tetrahydropteroylpolyglutamate: homocysteine methyltransferase; cobalamin-independent methionine synthase; methionine synthase (cobalamin-independent); MetE. Cat No: EXWM-1735. | |
| 6-carboxytetrahydropterin synthase | Binds Zn2+. Isolated from the bacteria Bacillus subtilis and Escherichia coli. The reaction is part of the biosynthesis pathway of queuosine.The enzyme from Escherichia coli can also convert 6-pyruvoyl-5,6,7,8-tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin. Group: Enzymes. Synonyms: CPH4 synthase; queD (gene name); ToyB; ykvK (gene name). Enzyme Commission Number: EC 4.1.2.50. 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-4887; 6-carboxytetrahydropterin synthase; EC 4.1.2.50; CPH4 synthase; queD (gene name); ToyB; ykvK (gene name). Cat No: EXWM-4887. | |
| acetate kinase | Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate. Group: Enzymes. Synonyms: acetokinase; AckA; AK; acetic kinase; acetate kinase (phosphorylating). Enzyme Commission Number: EC 2.7.2.1. CAS No. 9027-42-3. Acetate kinase. 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-3167; acetate kinase; EC 2.7.2.1; 9027-42-3; acetokinase; AckA; AK; acetic kinase; acetate kinase (phosphorylating). Cat No: EXWM-3167. | |
| alkanesulfonate monooxygenase | The enzyme from Escherichia coli catalyses the desulfonation of a wide range of aliphatic sulfonates (unsubstituted C1- to C14-sulfonates as well as substituted C2-sulfonates). Does not desulfonate taurine (2-aminoethanesulfonate) or aromatic sulfonates. Does not use FMN as a bound cofactor. Instead, it uses reduced FMN (i.e., FMNH2) as a substrate. FMNH2 is provided by SsuE, the associated FMN reductase (EC 1.5.1.38). Group: Enzymes. Synonyms: SsuD; sulfate starvation-induced protein 6; alkanesulfonate,reduced-FMN:oxygen oxidoreductase. Enzyme Commission Number: EC 1.14.14.5. CAS No. 256383-67-2. 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-0931; alkanesulfonate monooxygenase; EC 1.14.14.5; 256383-67-2; SsuD; sulfate starvation-induced protein 6; alkanesulfonate,reduced-FMN:oxygen oxidoreductase. Cat No: EXWM-0931. | |
| α-1,2-colitosyltransferase | The enzyme, characterized from the bacterium Escherichia coli O55:H7, participates in the biosynthesis of an O-antigen. The reaction involves anomeric inversion, and does not require any metal ions. The enzyme is highly specific towards the acceptor, exclusively recognizing lacto-N-biose, but can accept GDP-L-fucose as the donor with almost the same activity as with GDP-β-L-colitose. Group: Enzymes. Synonyms: wbgN (gene name). Enzyme Commission Number: EC 2.4.1.341. 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-2580; α-1,2-colitosyltransferase; EC 2.4.1.341; wbgN (gene name). Cat No: EXWM-2580. | |
| α-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase | Isolated from Escherichia coli. Involves an [4Fe-4S] cluster and a S-adenosyl-L-methionine (SAM) radical. Group: Enzymes. Synonyms: phnJ (gene name). Enzyme Commission Number: EC 4.7.1.1. 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-5357; α-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase; EC 4.7.1.1; phnJ (gene name). Cat No: EXWM-5357. | |
| α-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase | Isolated from the bacterium Escherichia coli. Group: Enzymes. Synonyms: phnM (gene name). Enzyme Commission Number: EC 3.6.1.63. 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-4636; α-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase; EC 3.6.1.63; phnM (gene name). Cat No: EXWM-4636. | |
| α-D-ribose 1-methylphosphonate 5-triphosphate synthase | Isolated from the bacterium Escherichia coli. Group: Enzymes. Enzyme Commission Number: EC 2.7.8.37. 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-3336; α-D-ribose 1-methylphosphonate 5-triphosphate synthase; EC 2.7.8.37. Cat No: EXWM-3336. | |
| α-Galactosidase, positionally specific from Escherichia coli, Recombinant | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Activity using maltose as substrate at ph 6.0 at 25 deg c is ~2x > that obtained using p-nitrophenyl-α-d-glucoside as substrate at ph 6.8 at 37 oc. protein determined by biuret. Applications: Α-glucosidase is potential enzyme for the biosynthesis of complex carbohydrates. Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. GLA. Activity: > 50 units/mg protein. Storage: 2-8°C. Form: Lyophilized powder containing potassium phosphate buffer salt. Source: E. coli. Species: Escherichia coli. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0293. | |
| asparagine synthase (glutamine-hydrolysing) | The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel. The enzyme catalyses three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. The C-terminal active site mediates both the synthesis of a β-aspartyl-AMP intermediate and its subsequent reaction with ammonia. The ammonia released is channeled to the other active site to yield asparagine. Group: Enzymes. Synonyms: asparagine synthetase (glutamine-hydrolysing); glutamine-dependent asparagine synthetase; asparagine synthetase B; AS; AS-B. Enzyme Commission Number: EC 6.3.5.4. CAS No. 37318-72-2. 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-5807; asparagine synthase (glutamine-hydrolysing); EC 6.3.5.4; 37318-72-2; asparagine synthetase (glutamine-hydrolysing); glutamine-dependent asparagine synthetase; asparagine synthetase B; AS; AS-B. Cat No: EXWM-5807. | |
| aspartate kinase | The enzyme from Escherichia coli is a multifunctional protein, which also catalyses the reaction of EC 1.1.1.3 homoserine dehydrogenase. This is also the case for two of the four isoenzymes in Arabidopsis thaliana. The equilibrium constant strongly favours the reaction from right to left, i.e. the non-physiological direction of reaction. Group: Enzymes. Synonyms: aspartokinase; AK; β-aspartokinase; aspartic kinase. Enzyme Commission Number: EC 2.7.2.4. CAS No. 9012-50-4. 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-3176; aspartate kinase; EC 2.7.2.4; 9012-50-4; aspartokinase; AK; β-aspartokinase; aspartic kinase. Cat No: EXWM-3176. | |
| Aspartate Kinase (Crude Enzyme) | Aspartate kinase (aspartokinase, aspartic kinase) is an enzyme that catalyzes the phosphorylation of the amino acid aspartate. This reaction is the first step in the biosynthesis of three essential amino acids: methionine, lysine, and threonine, known as the "aspartate family". The gene for aspartokinase is present only in microorganisms and plants; it is not present in animals, which must obtain aspartate-family amino acids in their diet. In Escherichia coli, aspartokinase is present as three independently regulated isozymes, each of which is specific to one of the three downstream biochemical pathways. This allows the independent regulation of the rates of methionine, lysin...pression by high concentrations of their end-products. Absence from animals makes these enzymes key targets for new herbicides and biocides and for improvements in nutritional value of crops. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Agriculture. Group: Enzymes. Synonyms: aspartokinase; AK; β-aspartokinase; aspartic kinase. Enzyme Commission Number: EC 2.7.2.4. CAS No. 9012-50-4. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. aspartokinase; AK; β-aspartokinase; aspartic kinase. Pack: 100ml. Cat No: NATE-1827. | |
| aspartate transaminase | A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis, some EC 2.6.1.57 activity can be found in this enzyme from other sources; indeed the enzymes are identical in Trichomonas vaginalis. Group: Enzymes. Synonyms: glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutarate-glutamate aminotransferase; aspartate α-ketoglutarate transaminase; aspartate aminotransferase; aspartate-2-oxoglutarate transaminase; aspartic acid aminotransferase; aspartic aminot. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. AST. 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-2839; aspartate transaminase; EC 2.6.1.1; 9000-97-9; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutarate-glutamate aminotransferase; aspartate α-ketoglutarate transaminase; aspartate aminotransferase; aspartate-2-oxoglutarate transaminase; aspartic acid aminotransferase; aspartic aminotransferase; aspartyl aminotransferase; AST; glutamate-oxalacetate aminotransferase; glutamate-oxalate transaminase; glutamic-aspartic a | |
| bacterial leucyl aminopeptidase | A zinc enzyme. Forms of the enzyme have been isolated from Aeromonas proteolytica, Escherichia coli and Streptococcus thermophilus. Examples are known from peptidase families M17 and M28 (of leucyl aminopeptidase and aminopeptidase Y, respectively). Group: Enzymes. Synonyms: Aeromonas proteolytica aminopeptidase. Enzyme Commission Number: EC 3.4.11.10. CAS No. 37288-67-8. Aminopeptidase. 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-4008; bacterial leucyl aminopeptidase; EC 3.4.11.10; 37288-67-8; Aeromonas proteolytica aminopeptidase. Cat No: EXWM-4008. | |
| β-Acetylglucosaminidase 18A from Bacteroides thetaiotaomicron, Recombinant | β-acetylglucosaminidase 18A, is an enzyme from Bacteroides thetaiotaomicron that participates in the endohydrolysis of the diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the (Man(GlcNAc)(2))Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Recombinant BtAcp18A (GH18), purified from Escherichia coli, is a single domain family 18 Glycoside Hydrolase (GH18). Group: Enzymes. Synonyms: beta-N-acetyl-D-hexosaminide; N-acetylhexosaminohydrolase; β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Purity: >50% by SDS-PAGE. β-N-Acetylhexosaminidase. Mole weight: 50.3 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacteroides thetaiotaomicron. beta-N-acetyl-D-hexosaminide; N-acetylhexosaminohydrolase; β-N-Acetylhexosaminidase; N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. Cat No: NATE-1291. | |
| carbamoyl-phosphate synthase (glutamine-hydrolysing) | The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 ? in length. The amidotransferase domain within the small subunit of the enzyme hydrolyses glutamine to ammonia via a thioester intermediate. The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large ... (gene name); CAD (gene name); hydrogen-carbonate:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating). Enzyme Commission Number: EC 6.3.5.5. CAS No. 37233-48-0. 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-5808; carbamoyl-phosphate synthase (glutamine-hydrolysing); EC 6.3.5.5; 37233-48-0; carbamoyl-phosphate synthetase (glutamine-hydrolysing); carbamyl phosphate synthetase (glutamine); carbamoylphosphate synthetase II; glutamine-dependent carbamyl phosphate synthetase; carbamoyl phosphate synthetase; CPS; carbon-dioxide:L-glutamine amido-ligase (ADP-forming, carbam | |
| chorismate lyase | This enzyme catalyses the first step in the biosynthesis of ubiquinone in Escherichia coli and other Gram-negative bacteria. The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine. Group: Enzymes. Synonyms: CL; CPL; UbiC. Enzyme Commission Number: EC 4.1.3.40. CAS No. 157482-18-3. 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-4917; chorismate lyase; EC 4.1.3.40; 157482-18-3; CL; CPL; UbiC. Cat No: EXWM-4917. | |
| citrate lyase holo-[acyl-carrier protein] synthase | The γ-subunit of EC 4.1.3.6, citrate (pro-3S) lyase, serves as an acyl-carrier protein (ACP) and contains the prosthetic group 2'-(5-triphosphoribosyl)-3'-dephospho-CoA. Synthesis and attachment of the prosthetic group requires the concerted action of this enzyme and EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase. In the enzyme from Escherichia coli, the prosthetic group is attached to serine-14 of the ACP via a phosphodiester bond. Group: Enzymes. Synonyms: 2'-(5''-phosphoribosyl)-3'-dephospho-CoA transferase; 2'-(5''-triphosphoribosyl)-3'-dephospho-Co. Enzyme Commission Number: EC 2.7.7.61. CAS No. 312492-44-7. 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-3273; citrate lyase holo-[acyl-carrier protein] synthase; EC 2.7.7.61; 312492-44-7; 2'-(5''-phosphoribosyl)-3'-dephospho-CoA transferase; 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase; CitX; holo-ACP synthase (ambiguous); 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase adenylyltransferase; 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA transferase; 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate-lyase adenylyltransferase; holo-citrate lyase synthase (incorrect). Cat No: EXWM-3273. | |
| CoA:oxalate CoA-transferase | The enzymes characterized from the bacteria Escherichia coli and Acetobacter aceti can also use formyl-CoA and oxalate (EC 2.8.3.16, formyl-CoA transferase) or formyl-CoA and acetate, with significantly reduced specific activities. Group: Enzymes. Synonyms: acetyl-coenzyme A transferase; acetyl-CoA oxalate CoA-transferase; ACOCT; YfdE; UctC. Enzyme Commission Number: EC 2.8.3.19. 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-3414; CoA:oxalate CoA-transferase; EC 2.8.3.19; acetyl-coenzyme A transferase; acetyl-CoA oxalate CoA-transferase; ACOCT; YfdE; UctC. Cat No: EXWM-3414. | |
| D-amino acid dehydrogenase (quinone) | An iron-sulfur flavoprotein (FAD). The enzyme from the bacterium Helicobacter pylori is highly specific for D-proline, while the enzyme from the bacterium Escherichia coli B is most active with D-alanine, D-phenylalanine and D-methionine. This enzyme may be the same as EC 1.4.99.6. Group: Enzymes. Synonyms: DadA. Enzyme Commission Number: EC 1.4.5.1. 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-1486; D-amino acid dehydrogenase (quinone); EC 1.4.5.1; DadA. Cat No: EXWM-1486. | |
| D-aminoacyl-tRNA deacylase | The enzyme from Escherichia coli can cleave D-tyrosyl-tRNATyr, D-aspartyl-tRNAAsp and D-tryptophanyl-tRNATrp. Whereas the enzyme from the archaeon Pyrococcus abyssi is a zinc protein, the enzyme from Escherichia coli does not carry any zinc. Group: Enzymes. Synonyms: Dtd2; D-Tyr-tRNA(Tyr) deacylase; D-Tyr-tRNATyr deacylase; D-tyrosyl-tRNATyr aminoacylhydrolase; dtdA (gene name). Enzyme Commission Number: EC 3.1.1.96. 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-3525; D-aminoacyl-tRNA deacylase; EC 3.1.1.96; Dtd2; D-Tyr-tRNA(Tyr) deacylase; D-Tyr-tRNATyr deacylase; D-tyrosyl-tRNATyr aminoacylhydrolase; dtdA (gene name). Cat No: EXWM-3525. | |
| D-arabinose isomerase | Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+). The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism. The enzyme catalyses the aldose-ketose isomerization of several sugars. Most enzymes also catalyse the reaction of EC 5.3.1.25, L-fucose isomerase. The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose. cf. EC 5.3.1.4, L-arabinose isomerase. Group: Enzymes. Synonyms: D-arabinose(L-fucose) isomerase; L-fucose isomerase; D-arabinose ketol-isomerase; arabinose isomerase (misleading). Enzyme Commission Number: EC 5.3.1.3. CAS No. 9023-81-8. 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-5469; D-arabinose isomerase; EC 5.3.1.3; 9023-81-8; D-arabinose(L-fucose) isomerase; L-fucose isomerase; D-arabinose ketol-isomerase; arabinose isomerase (misleading). Cat No: EXWM-5469. | |
| (d)CTP diphosphatase | The enzyme, characterized from the bacterium Escherichia coli, is specific for the pyrimidine nucleotides CTP and dCTP. It also acts on 5-methyl-dCTP, 5-hydroxy-dCTP and 8-hydroxy-dGTP. Group: Enzymes. Synonyms: (d)CTP pyrophosphohydrolase; (d)CTP diphosphohydrolase; nudG (gene name). Enzyme Commission Number: EC 3.6.1.65. 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-4638; (d)CTP diphosphatase; EC 3.6.1.65; (d)CTP pyrophosphohydrolase; (d)CTP diphosphohydrolase; nudG (gene name). Cat No: EXWM-4638. | |
| demethylmenaquinone methyltransferase | The enzyme catalyses the last step in menaquinone biosynthesis. It is able to accept substrates with varying polyprenyl side chain length (the chain length is determined by polyprenyl diphosphate synthase). The enzyme from Escherichia coli also catalyses the conversion of 2-methoxy-6-octaprenyl-1,4-benzoquinone to 5-methoxy-2-methyl-3-octaprenyl-1,4-benzoquinone during the biosynthesis of ubiquinone. The enzyme probably acts on menaquinol rather than menaquinone. Group: Enzymes. Synonyms: S-adenosyl-L-methione-DMK methyltransferase; demethylmenaquinone C-methylase; 2-heptaprenyl-1,4-naphthoquinone methyltransferase; 2-demethylmenaquinone methyltransferase; S-adenosyl-L-methione:2-demethylmenaquinone methyltransferase. Enzyme Commission Number: EC 2.1.1.163. 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-1760; demethylmenaquinone methyltransferase; EC 2.1.1.163; S-adenosyl-L-methione-DMK methyltransferase; demethylmenaquinone C-methylase; 2-heptaprenyl-1,4-naphthoquinone methyltransferase; 2-demethylmenaquinone methyltransferase; S-adenosyl-L-methione:2-demethylmenaquinone methyltransferase. Cat No: EXWM-1760. | |
| deoxynucleotide 3'-phosphatase | Also catalyses the selective removal of 3'-phosphate groups from DNA and oligodeoxyribonucleotides. Induced in Escherichia coli by T-even phages. Group: Enzymes. Synonyms: 3'-deoxynucleotidase; 3'-deoxyribonucleotidase. Enzyme Commission Number: EC 3.1.3.34. CAS No. 37288-18-9. 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-3637; deoxynucleotide 3'-phosphatase; EC 3.1.3.34; 37288-18-9; 3'-deoxynucleotidase; 3'-deoxyribonucleotidase. Cat No: EXWM-3637. | |
| dihydroneopterin aldolase | The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis. The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyse the epimerisation of the 2' hydroxy-group (EC 5.1.99.8, 7,8-dihydroneopterin epimerase). The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyses EC 5.1.99.8 and EC 1.13.11.81, 7,8-dihydroneopterin oxygenase. The enzyme from the yeast Saccharomyces cerevisiae also catalyses the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3, 2-amino-4-hydroxy-6-(hydroxymethyl)dihydropteridine diphosphokinase, and EC 2.5.1.15, dihydropteroate synthase. Group: Enzymes. Synonyms: 7,8-dihydroneopterin aldolase; 2-amino-. Enzyme Commission Number: EC 4.1.2.25. CAS No. 37290-59-8. 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-4864; dihydroneopterin aldolase; EC 4.1.2.25; 37290-59-8; 7,8-dihydroneopterin aldolase; 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase; 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-forming); DHNA; mptD (gene name); folB (gene name). Cat No: EXWM-4864. | |
| DNA-3-methyladenine glycosylase I | Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA-[protein]-cysteine S-methyltransferase). Group: Enzymes. Synonyms: deoxyribonucleate 3-methyladenine glycosidase I; 3-methyladenine DNA glycosylase I; DNA-3-methyladenine glycosidase I. Enzyme Commission Number: EC 3.2.2.20. CAS No. 89287-37-6. 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-3974; DNA-3-methyladenine glycosylase I; EC 3.2.2.20; 89287-37-6; deoxyribonucleate 3-methyladenine glycosidase I; 3-methyladenine DNA glycosylase I; DNA-3-methyladenine glycosidase I. Cat No: EXWM-3974. | |
| DNA-3-methyladenine glycosylase II | Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA-[protein]-cysteine S-methyltransferase). Group: Enzymes. Synonyms: deoxyribonucleate 3-methyladenine glycosidase II; 3-methyladenine DNA glycosylase II; DNA-3-methyladenine glycosidase II; AlkA. Enzyme Commission Number: EC 3.2.2.21. CAS No. 89287-38-7. 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-3975; DNA-3-methyladenine glycosylase II; EC 3.2.2.21; 89287-38-7; deoxyribonucleate 3-methyladenine glycosidase II; 3-methyladenine DNA glycosylase II; DNA-3-methyladenine glycosidase II; AlkA. Cat No: EXWM-3975. | |
| dTDP-4-dehydro-6-deoxyglucose reductase | The enzymes from the Gram-negative bacteria Aggregatibacter actinomycetemcomitans and Escherichia coli O52 are involved in activation of fucose for incorporation into capsular polysaccharide O-antigens. The enzyme from the Gram-positive bacterium Anoxybacillus tepidamans (Geobacillus tepidamans) is involved in activation of fucose for incorporation into the organism's S-layer. The enzyme from Escherichia coli O52 has a higher catalytic efficiency with NADH than with NADPH. Group: Enzymes. Synonyms: dTDP-4-keto-6-deoxyglucose reductase; dTDP-D-fucose:NADP+ oxidoreductase; Fcf1; dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase. Enzyme Commission Number: EC 1.1.1.266. 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-0172; dTDP-4-dehydro-6-deoxyglucose reductase; EC 1.1.1.266; dTDP-4-keto-6-deoxyglucose reductase; dTDP-D-fucose:NADP+ oxidoreductase; Fcf1; dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase. Cat No: EXWM-0172. | |
| EcoR I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 40-fold overdigestion with enzyme about 95% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 5000U; 25000U. G↑AATTC CTTAA↓G. Activity: 20000; 50000u.a./ml. Appearance: 10 X SE-buffer EcoRI, BSA. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned EcoR I gene from Escherichia coli. Pack: 10 mM Tris-HCl (pH 7.5); 200 mM NaCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1101RE. | |
| EcoR V | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 20-fold overdigestion with enzyme 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 2000U; 10000U. GAT↑ATC CTA↓TAG. Activity: 20000u.a./ml. Appearance: 10 X SE-buffer W, BSA. Storage: -20°C. Form: Liquid. Source: An E.coli strain, that carries the cloned gene EcoRV from Escherichia coli. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM NaCl; 0,1 mM EDTA; 1 mM DTT; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1102RE. | |
| enoyl-[acyl-carrier-protein] reductase (NADH) | The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18. The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons. Group: Enzymes. Synonyms: enoyl-[acyl carrier protein] reductase; enoyl-ACP reductase; NADH-enoyl acyl carrier protein reductase; NADH-specific enoyl-ACP reductase; acyl-[acyl-carrier-protein]:NAD+ oxidoreductase; fabI (gene name); inhA (gene name). Enzyme Commission Number: EC 1.3.1.9. CAS No. 37251-08-4. 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-1359; enoyl-[acyl-carrier-protein] reductase (NADH); EC 1.3.1.9; 37251-08-4; enoyl-[acyl carrier protein] reductase; enoyl-ACP reductase; NADH-enoyl acyl carrier protein reductase; NADH-specific enoyl-ACP reductase; acyl-[acyl-carrier-protein]:NAD+ oxidoreductase; fabI (gene name); inhA (gene name). Cat No: EXWM-1359. | |
| Enterokinase from bovine intestine, Recombinant | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is a member of the s1 peptidase family. in vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. enterokinase is used for site specific ...yme from creative enzymes has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed in escherichia coli. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 28 kDa light chain form. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: Type I, supplied as a solution in 20 mM Tris-HCl, 200 mM NaCl, and 50% glycerol; Type II, white powder. Source: E. coli. Species: Bovine intestine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Pack: vial of ~0.2 unit. Cat No: NATE-0226. | |
| 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. | |
| flavin reductase (NADH) | The enzyme from Escherichia coli W catalyses the reduction of free flavins by NADH. The enzyme has similar affinity to FAD, FMN and riboflavin. Activity with NADPH is more than 2 orders of magnitude lower than activity with NADH. Group: Enzymes. Synonyms: NADH-dependent flavin reductase; flavin:NADH oxidoreductase. Enzyme Commission Number: EC 1.5.1.36. 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-1517; flavin reductase (NADH); EC 1.5.1.36; NADH-dependent flavin reductase; flavin:NADH oxidoreductase. Cat No: EXWM-1517. | |
| FMN reductase (NADPH) | The enzymes from bioluminescent bacteria contain FMN, while the enzyme from Escherichia coli does not. The enzyme often forms a two-component system with monooxygenases such as luciferase. Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor. While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity. Group: Enzymes. Synonyms: FRP; flavin reductase P; SsuE. Enzyme Commission Number: EC 1.5.1.38. 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-1519; FMN reductase (NADPH); EC 1.5.1.38; FRP; flavin reductase P; SsuE. Cat No: EXWM-1519. | |
| Fpg Protein from Escherichia coli, Recombinant | Fpg protein, a key enzyme in the DNA base excision repair pathway (BER), catalyses the excision of a broad spectrum of modified purines such as formamidopyrimidine (Fapy) and 8-oxoguanine (8-oxo-G). Fpg possess both DNA glycosylase activity that removes the mutated base and AP-lyase activity that releases ribose, leaving both 5'-and 3'-phosphorylated ends in the DNA. Several analytical methods based on Fpg protein activity in vitro were developed for detection and quantitation of oxidative damage to DNA mainly for FapyA, FapyG and 8-oxo-G. The fpg gene was cloned by Boiteux, et al. Fpg protein possess a zinc finger motif at its C-terminus (one zinc atom per molecule). ... Protein. Mole weight: mol wt 30.2 kDa (269 amino acids, predicted from the nucleotide sequence). Activity: >20 ,000 units/mg protein. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 50 mM potassium HEPES, pH 7.5, 1 mM DTT, 1 mM EDTA, and 200 mM NaCl. Source: E. coli. Species: Escherichia coli. Fapy-DNA glycosylase; deoxyribonucleate glycosidase; 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase; 2,6-diamino-4-hydroxy-5 (N-methyl)formamidopyrimidine-DNA glycosylase; formamidopyrimidine-DNA glycosylase; DNA-formamidopyrimidine glycosidase; Fpg protein; DNA-formamidopyrimidine glycosylase; EC 3.2.2.23; 78783-53-6; | |
| galactarate dehydratase | The enzyme from the bacterium Escherichia coli is specific for galactarate, while the enzyme from Salmonella typhimurium also has activity with L-talarate (cf. EC 4.2.1.156, L-talarate dehydratase). cf. EC 4.2.1.158, galactarate dehydratase (D-threo-forming). Group: Enzymes. Synonyms: D-galactarate hydro-lyase; D-galactarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming); talrD (gene name)/galrD (gene name); galactarate dehydratase (L-threo-forming). Enzyme Commission Number: EC 4.2.1.42. CAS No. 37290-78-1. 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-5031; galactarate dehydratase; EC 4.2.1.42; 37290-78-1; D-galactarate hydro-lyase; D-galactarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming); talrD (gene name)/galrD (gene name); galactarate dehydratase (L-threo-forming). Cat No: EXWM-5031. | |
| galactokinase | Part of the Leloir pathway for galactose metabolism. The enzymes from mammals and from the bacterium Escherichia coli have no activity with N-acetyl-α-D-galactosamine. Group: Enzymes. Synonyms: galactokinase (phosphorylating); ATP:D-galactose-1-phosphotransferase. Enzyme Commission Number: EC 2.7.1.6. CAS No. 9030-53-9. GALK. 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-3090; galactokinase; EC 2.7.1.6; 9030-53-9; galactokinase (phosphorylating); ATP:D-galactose-1-phosphotransferase. Cat No: EXWM-3090. | |
| 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. | |
| 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 dehydrogenase [NAD(P)+] | The enzyme from Escherichia coli shows specificity for the B side of NADPH. Group: Enzymes. Synonyms: L-glycerol-3-phosphate:NAD(P) oxidoreductase; glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate)); glycerol 3-phosphate dehydrogenase (NADP); glycerol-3-phosphate dehydrogenase [NAD(P)]. Enzyme Commission Number: EC 1.1.1.94. CAS No. 37250-30-9. 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-0378; glycerol-3-phosphate dehydrogenase [NAD(P)+]; EC 1.1.1.94; 37250-30-9; L-glycerol-3-phosphate:NAD(P) oxidoreductase; glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate)); glycerol 3-phosphate dehydrogenase (NADP); glycerol-3-phosphate dehydrogenase [NAD(P)]. Cat No: EXWM-0378. | |
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