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| Product | Description | |
|---|---|---|
| 2,3-bisphosphoglycerate 3-phosphatase | This reaction is a shortcut in the Rapoport-Luebering shunt. It bypasses the reactions of EC 3.1.3.13/EC 5.4.2.12 [bisphosphoglycerate phosphatase/phosphoglycerate mutase (2,3-diphosphoglycerate-independent)] and directly forms 2-phospho-D-glycerate by removing the 3-phospho-group of 2,3-diphospho-D-glycerate. The MIPP1 protein also catalyses the reaction of EC 3.1.3.62 (multiple inositol-polyphosphate phosphatase). Group: Enzymes. Synonyms: MIPP1; 2,3-BPG 3-phosphatase. Enzyme Commission Number: EC 3.1.3.80. 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-3686; 2,3-bisphosphoglycerate 3-phosphatase; EC 3.1.3.80; MIPP1; 2,3-BPG 3-phosphatase. Cat No: EXWM-3686. |  |
| 2,3-Diphospho-D-glyceric acid penta(cyclohexylammonium) salt | D-Glycerate 2,3-diphosphate (DPG), cofactor of both phosphoglyceric acid mutase and hemoglobin, may be used as a reference compound in analysis of blood cell (erythrocyte) glycolysic cycle metabolites. 2,3-diphosphoglycerate (DPG) may be used as a reference in assays that measure DPG levels to indicate the health status of erythrocytes/red blood cells (RBC). Applications: Used as a reference compound in analysis of blood cell (erythrocyte) glycolysic cycle metabolites. Group: Coenzymes. Synonyms: D-Glycerate 2,3-diphosphate pentacyclohexylamine salt. CAS No. 62868-79-5. Purity: ≥95%. Mole weight: 761.91. Appearance: Powder. Form: Solid. D-Glycerate 2,3-diphosphate pentacyclohexylamine salt; 2,3-Diphospho-D-glyceric acid penta(cyclohexylammonium) salt; 62868-79-5. Cat No: COEC-080. | |
| 2-acetolactate mutase | Requires ascorbic acid; also converts 2-aceto-2-hydroxybutanoate to 3-hydroxy-3-methyl-2-oxopentanoate. Group: Enzymes. Synonyms: acetolactate mutase; acetohydroxy acid isomerase. Enzyme Commission Number: EC 5.4.99.3. CAS No. 37318-52-8. 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-5570; 2-acetolactate mutase; EC 5.4.99.3; 37318-52-8; acetolactate mutase; acetohydroxy acid isomerase. Cat No: EXWM-5570. | |
| 2-hydroxyisobutanoyl-CoA mutase | The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, uses radical chemistry to rearrange the positions of both a methyl group and a hydroxyl group. It consists of two subunits, the smaller one containing a cobalamin cofactor. It plays a central role in the degradation of assorted substrates containing a tert-butyl moiety. Group: Enzymes. Synonyms: hcmAB (gene names). Enzyme Commission Number: EC 5.3.3.20. 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-5499; 2-hydroxyisobutanoyl-CoA mutase; EC 5.3.3.20; hcmAB (gene names). Cat No: EXWM-5499. | |
| 2-hydroxymethylglutarate dehydrogenase | NADP+ cannot replace NAD+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 3.5.2.18 (enamidase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase). Group: Enzymes. Synonyms: HgD. Enzyme Commission Number: EC 1.1.1.291. CAS No. 1073478-76-8. 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-0200; 2-hydroxymethylglutarate dehydrogenase; EC 1.1.1.291; 1073478-76-8; HgD. Cat No: EXWM-0200. | |
| 2-methyleneglutarate mutase | Requires a cobamide coenzyme. Group: Enzymes. Synonyms: α-methyleneglutarate mutase. Enzyme Commission Number: EC 5.4.99.4. CAS No. 9059-10-3. 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-5581; 2-methyleneglutarate mutase; EC 5.4.99.4; 9059-10-3; α-methyleneglutarate mutase. Cat No: EXWM-5581. | |
| 3-(hydroxyamino)phenol mutase | This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring hydroxy groups. Group: Enzymes. Synonyms: 3-hydroxylaminophenol mutase; 3HAP mutase. Enzyme Commission Number: EC 5.4.4.3. CAS No. 224427-05-8. 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-5544; 3-(hydroxyamino)phenol mutase; EC 5.4.4.3; 224427-05-8; 3-hydroxylaminophenol mutase; 3HAP mutase. Cat No: EXWM-5544. | |
| 4-carboxymethyl-4-methylbutenolide mutase | This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. Group: Enzymes. Synonyms: 4-methyl-2-enelactone isomerase; 4-methylmuconolactone methylisomerase; 4-methyl-3-enelactone methyl isomerase. Enzyme Commission Number: EC 5.4.99.14. CAS No. 115300-03-3. 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-5553; 4-carboxymethyl-4-methylbutenolide mutase; EC 5.4.99.14; 115300-03-3; 4-methyl-2-enelactone isomerase; 4-methylmuconolactone methylisomerase; 4-methyl-3-enelactone methyl isomerase. Cat No: EXWM-5553. | |
| 5-(carboxyamino)imidazole ribonucleotide mutase | In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase, is required to carry out the single reaction catalysed by EC 4.1.1.21, phosphoribosylaminoimidazole carboxylase, in vertebrates. In the absence of EC 6.3.2.6, phosphoribosyl aminoimidazolesuccinocarboxamide synthase, the reaction is reversible. The substrate is readily converted into 5-amino-1-(5-phospho-D-ribosyl)imidazole by non-enzymic decarboxylation. Group: Enzymes. Synonyms: N5-CAIR mutase; PurE; N5-carboxyaminoimidazole ribonucleotide mutase; class I PurE. Enzyme Commission Number: EC 5.4.99.18. CAS No. 255379-40-9. 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-5557; 5-(carboxyamino)imidazole ribonucleotide mutase; EC 5.4.99.18; 255379-40-9; N5-CAIR mutase; PurE; N5-carboxyaminoimidazole ribonucleotide mutase; class I PurE. Cat No: EXWM-5557. | |
| 5-(carboxyamino)imidazole ribonucleotide synthase | In Escherichia coli, this enzyme, along with EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase, is required to carry out the single reaction catalysed by EC 4.1.1.21, phosphoribosylaminoimidazole carboxylase, in vertebrates. Belongs to the ATP grasp protein superfamily. Carboxyphosphate is the putative acyl phosphate intermediate. Involved in the late stages of purine biosynthesis. Group: Enzymes. Synonyms: N5-CAIR synthetase; N5-carboxyaminoimidazole ribonucleotide synthetase; PurK. Enzyme Commission Number: EC 6.3.4.18. CAS No. 255379-40-9. 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-5787; 5-(carboxyamino)imidazole ribonucleotide synthase; EC 6.3.4.18; 255379-40-9; N5-CAIR synthetase; N5-carboxyaminoimidazole ribonucleotide synthetase; PurK. Cat No: EXWM-5787. | |
| 5-Isopropyl-3-methylphenol | 5-Isopropyl-3-methylphenol is a derivative of Carvacrol (C184600); a major phenolic component of oregano oil and a novel inhibitor of the Mycobacterium tuberculosis (MTB) chorismate mutase (CM) enzyme. Group: Biochemicals. Grades: Highly Purified. CAS No. 3228-3-3. Pack Sizes: 2.5g, 25g. Molecular Formula: C10H14O, Molecular Weight: 150.22. US Biological Life Sciences. |  Worldwide |
| 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase | The enzyme contains heme. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60, linoleate 8R-lipoxygenase), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate within the C-terminal P-450 heme thiolate domain. Group: Enzymes. Synonyms: 5,8-LDS (bifunctional enzyme); 5,8-linoleate diol synthase (bifunctional enzyme); 8-hydroperoxide isomerase; (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate-forming); PpoA. Enzyme Commission Number: EC 5.4.4.5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5546; 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase; EC 5.4.4.5; 5,8-LDS (bifunctional enzyme); 5,8-linoleate diol synthase (bifunctional enzyme); 8-hydroperoxide isomerase; (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate-forming); PpoA. Cat No: EXWM-5546. | |
| 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase | The enzyme contains heme. The bifunctional enzyme from Gaeumannomyces graminis catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60, linoleate 8R-lipoxygenase), which is then isomerized to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate. Group: Enzymes. Synonyms: 8-hydroperoxide isomerase (ambiguous); (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate-forming). Enzyme Commission Number: EC 5.4.4.6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5547; 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase; EC 5.4.4.6; 8-hydroperoxide isomerase (ambiguous); (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate mutase ((7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate-forming). Cat No: EXWM-5547. | |
| β-lysine 5,6-aminomutase | Requires a cobamide coenzyme. Group: Enzymes. Synonyms: β-lysine mutase; L-β-lysine 5,6-aminomutase. Enzyme Commission Number: EC 5.4.3.3. CAS No. 9075-69-8. 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-5535; β-lysine 5,6-aminomutase; EC 5.4.3.3; 9075-69-8; β-lysine mutase; L-β-lysine 5,6-aminomutase. Cat No: EXWM-5535. | |
| bisphosphoglycerate mutase | In the direction shown, this enzyme is phosphorylated by 3-phosphoglyceroyl phosphate, to give phosphoenzyme and 3-phosphoglycerate. The latter is rephosphorylated by the enzyme to yield 2,3-bisphosphoglycerate, but this reaction is slowed by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. This enzyme also catalyses, slowly, the reactions of EC 3.1.3.13 (bisphosphoglycerate phosphatase), EC 5.4.2.11 [phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)] and EC 5.4.2.12 [phosphoglycerate mutase (2,3-diphosphoglycerate-independent)]. Group: Enzymes. Synonyms: diphosphoglycerate mutase; glycerate phosphomutase; bisphosphoglycerate synthase; bisphosphoglyceromutase; bip. Enzyme Commission Number: EC 5.4.2.4. CAS No. 37211-69-1. 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-5526; bisphosphoglycerate mutase; EC 5.4.2.4; 37211-69-1; diphosphoglycerate mutase; glycerate phosphomutase; bisphosphoglycerate synthase; bisphosphoglyceromutase; biphosphoglycerate synthase; diphosphoglyceric mutase; 2,3-diphosphoglycerate mutase; phosphoglyceromutase; 2,3-diphosphoglycerate synthase; DPGM; 2,3-bisphosphoglycerate mutase; BPGM; diphosphoglyceromutase; 2,3-diphosphoglyceromutase. Cat No: EXWM-5526. | |
| chorismate mutase | In enzymology, a chorismate mutase (EC 5.4.99.5) is an enzyme that catalyzes the chemical reaction for the conversion of chorismate to prephenate in the pathway to the production of phenylalanine and tyrosine, also known as the shikimate pathway. Group: Enzymes. Synonyms: hydroxyphenylpyruvate synthase. Enzyme Commission Number: EC 5.4.99.5. CAS No. 9068-30-8. 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-5592; chorismate mutase; EC 5.4.99.5; 9068-30-8; hydroxyphenylpyruvate synthase. Cat No: EXWM-5592. | |
| cucurbitadienol synthase | This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. Group: Enzymes. Synonyms: CPQ (gene name); (S)-2,3-epoxysqualene mutase (cyclizing, cucurbitadienol-forming). Enzyme Commission Number: EC 5.4.99.33. 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-5574; cucurbitadienol synthase; EC 5.4.99.33; CPQ (gene name); (S)-2,3-epoxysqualene mutase (cyclizing, cucurbitadienol-forming). Cat No: EXWM-5574. | |
| cycloartenol synthase | This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. This enzyme participates in biosynthesis of steroids. Group: Enzymes. Synonyms: 2,3-epoxysqualene cycloartenol-cyclase; squalene-2,3-epoxide-cycloartenol cyclase; 2,3-epoxysqualene-cycloartenol cyclase; 2,3-oxidosqualene-cycloartenol cyclase; (S)-2,3-epoxysqualene mutase (cyclizing, cycloartenol-forming). Enzyme Commission Number: EC 5.4.99.8. CAS No. 9075-25-6. 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-5608; cycloartenol synthase; EC 5.4.99.8; 9075-25-6; 2,3-epoxysqualene cycloartenol-cyclase; squalene-2,3-epoxide-cycloartenol cyclase; 2,3-epoxysqualene-cycloartenol cyclase; 2,3-oxidosqualene-cycloartenol cyclase; (S)-2,3-epoxysqualene mutase (cyclizing, cycloartenol-forming). Cat No: EXWM-5608. | |
| D-(+)-2-Phosphoglyceric Acid Sodium Hydrate | Enantiomerically pure metabolite of glycolysis / gluconeogenesis and also substrate for a number of important enzymes in central metabolism like enolase and phosphoglycerate mutase. Group: Biochemicals. Alternative Names: (R) -3-Hydroxy-2- (phosphonooxy) propanoic Acid Trisodium Salt. Grades: Highly Purified. CAS No. 70195-25-4. Pack Sizes: 5mg, 10mg. Molecular Formula: C?H?Na?O?P, Molecular Weight: 252. US Biological Life Sciences. | Worldwide |
| D-lysine 5,6-aminomutase | Requires a cobamide coenzyme. Group: Enzymes. Synonyms: D-α-lysine mutase; adenosylcobalamin-dependent D-lysine 5,6-aminomutase. Enzyme Commission Number: EC 5.4.3.4. CAS No. 9075-70-1. 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-5536; D-lysine 5,6-aminomutase; EC 5.4.3.4; 9075-70-1; D-α-lysine mutase; adenosylcobalamin-dependent D-lysine 5,6-aminomutase. Cat No: EXWM-5536. | |
| dTDP-fucopyranose mutase | The enzyme is involved in the biosynthesis of the Escherichia coli O52 O antigen. Group: Enzymes. Synonyms: Fcf2. Enzyme Commission Number: EC 5.4.99.59. 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-5602; dTDP-fucopyranose mutase; EC 5.4.99.59; Fcf2. Cat No: EXWM-5602. | |
| enamidase | Contains iron and Zn2+.Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 1.1.1.291 (2-hydroxymethylglutarate dehydrogenase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase). Group: Enzymes. Enzyme Commission Number: EC 3.5.2.18. 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-4501; enamidase; EC 3.5.2.18. Cat No: EXWM-4501. | |
| ethylmalonyl-CoA mutase | The enzyme, characterized from the bacterium Rhodobacter sphaeroides, is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation. Requires coenzyme B12 for activity. Group: Enzymes. Synonyms: Ecm. Enzyme Commission Number: EC 5.4.99.63. 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-5606; ethylmalonyl-CoA mutase; EC 5.4.99.63; Ecm. Cat No: EXWM-5606. | |
| germanicol synthase | The enzyme produces germanicol, β-amyrin and lupeol in the ratio 63:33:4. Group: Enzymes. Synonyms: RsM1; (S)-2,3-epoxysqualene mutase (cyclizing, germanicol-forming). Enzyme Commission Number: EC 5.4.99.34. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5575; germanicol synthase; EC 5.4.99.34; RsM1; (S)-2,3-epoxysqualene mutase (cyclizing, germanicol-forming). Cat No: EXWM-5575. | |
| Glyoxalase I from Human, Recombinant | Glyoxalase I is universally expressed and involved in the protection against cellular damage due to cytotoxic metabolites such as advanced glycation end products (AGEs). It is an integral component of the detoxification system, catalyzing the conversion of reactive, acyclic a-oxoaldehydes into the corresponding a-hydroxyacids in a glutathione-dependent manner. Group: Enzymes. Synonyms: lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Enzyme Commission Number: EC 4.4.1.5. Purity: > 90% by SDS-PAGE. Glyoxalase I. Mole weight: 20.7 kDa. Activity: >0.4 units/mg. Storage: Glyoxalase-I Human Recombinant although stable at 4 °C for weeks, should be stored desiccated below -18 °C. Please prevent freeze/thaw cycles. Form: Glyoxalase-1 solution containing 20 mM Tris pH-8, 1mM DTT and 10% glycerol. Source: E. coli. Species: Human. lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Cat No: NATE-1651. | |
| (hydroxyamino)benzene mutase | This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring hydroxy groups. This enzyme participates in naphthalene and anthracene degradation. Group: Enzymes. Synonyms: HAB mutase; hydroxylaminobenzene hydroxymutase; hydroxylaminobenzene mutase. Enzyme Commission Number: EC 5.4.4.1. CAS No. 261765-91-7. 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-5542; (hydroxyamino)benzene mutase; EC 5.4.4.1; 261765-91-7; HAB mutase; hydroxylaminobenzene hydroxymutase; hydroxylaminobenzene mutase. Cat No: EXWM-5542. | |
| isobutyryl-CoA mutase | Requires a cobamide coenzyme. Group: Enzymes. Synonyms: isobutyryl coenzyme A mutase; butyryl-CoA:isobutyryl-CoA mutase. Enzyme Commission Number: EC 5.4.99.13. CAS No. 116405-23-3. 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-5552; isobutyryl-CoA mutase; EC 5.4.99.13; 116405-23-3; isobutyryl coenzyme A mutase; butyryl-CoA:isobutyryl-CoA mutase. Cat No: EXWM-5552. | |
| Isobutyryl coenzyme A lithium salt | Isobutyryl coenzyme A lithium salt is an acyl group carrier. Isobutyryl coenzyme A (IB-CoA), a short-chain branched acyl-CoA, provides the starter unit for biosynthesis of myxalamid B. Isobutyryl coenzyme A is used as a substrate to study the specificity and kinetics of isobutyryl-coenzyme A (CoA) mutase. Applications: An acyl group carrier. Group: Coenzymes. Synonyms: IB-CoA. CAS No. 103404-95-1. Purity: ≥85%. Mole weight: 837.62 (free acid basis). Appearance: Powder. Form: Solid. IB-CoA; Isobutyryl coenzyme A lithium salt; 103404-95-1. Cat No: COEC-055. | |
| isomultiflorenol synthase | This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. Group: Enzymes. Synonyms: LcIMS1; (S)-2,3-epoxysqualene mutase (cyclizing, isomultiflorenol-forming). Enzyme Commission Number: EC 5.4.99.36. 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-5577; isomultiflorenol synthase; EC 5.4.99.36; LcIMS1; (S)-2,3-epoxysqualene mutase (cyclizing, isomultiflorenol-forming). Cat No: EXWM-5577. | |
| lactoylglutathione lyase | Also acts on 3-phosphoglycerol-glutathione. Group: Enzymes. Synonyms: methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing). Enzyme Commission Number: EC 4.4.1.5. CAS No. 9033-12-9. Glyoxalase I. 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-5339; lactoylglutathione lyase; EC 4.4.1.5; 9033-12-9; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing). Cat No: EXWM-5339. | |
| lanosterol synthase | Lanosterol synthase is an oxidosqualene cyclase (OSC) enzyme that converts (S)-2,3-oxidosqualene to a protosterol cation and finally to lanosterol. Lanosterol is a key four-ringed intermediate in cholesterol biosynthesis. In humans, lanosterol synthase is encoded by the LSS gene. Group: Enzymes. Synonyms: 2,3-epoxysqualene lanosterol cyclase; squalene-2,3-oxide-lanosterol cyclase; lanosterol 2,3-oxidosqualene cyclase; squalene 2,3-epoxide:lanosterol cyclase; 2,3-oxidosqualene sterol cyclase; oxidosqualene cyclase; 2,3-oxidosqualene cyclase; 2,3-oxidosqualene-lanosterol cyclase; oxidosqualene-lanosterol cyclase; squalene epoxidase-cyclase; (S)-2,3-epoxysqualene mutase (cyclizing, lanosterol-forming). Enzyme Commission Number: EC 5.4.99.7. CAS No. 9032-71-7. 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-5607; lanosterol synthase; EC 5.4.99.7; 9032-71-7; 2,3-epoxysqualene lanosterol cyclase; squalene-2,3-oxide-lanosterol cyclase; lanosterol 2,3-oxidosqualene cyclase; squalene 2,3-epoxide:lanosterol cyclase; 2,3-oxidosqualene sterol cyclase; oxidosqualene cyclase; 2,3-oxidosqualene cyclase; 2,3-oxidosqualene-lanosterol cyclase; oxidosqualene-lanosterol cyclase; squalene epoxidase-cyclase; (S)-2,3-epoxysqualene mutase (cyclizing, lanosterol-forming). Cat No: EXWM-5607. | |
| methylaspartate mutase | Requires a cobamide coenzyme. Group: Enzymes. Synonyms: glutamate mutase; glutamic mutase; glutamic isomerase; glutamic acid mutase; glutamic acid isomerase; methylaspartic acid mutase; β-methylaspartate-glutamate mutase; glutamate isomerase. Enzyme Commission Number: EC 5.4.99.1. CAS No. 9032-97-7. 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-5549; methylaspartate mutase; EC 5.4.99.1; 9032-97-7; glutamate mutase; glutamic mutase; glutamic isomerase; glutamic acid mutase; glutamic acid isomerase; methylaspartic acid mutase; β-methylaspartate-glutamate mutase; glutamate isomerase. Cat No: EXWM-5549. | |
| methylmalonyl-CoA mutase | Requires a cobamide coenzyme. Group: Enzymes. Synonyms: methylmalonyl-CoA CoA-carbonyl mutase; methylmalonyl coenzyme A mutase; methylmalonyl coenzyme A carbonylmutase; (S)-methylmalonyl-CoA mutase; (R)-2-methyl-3-oxopropanoyl-CoA CoA-carbonylmutase [incorrect]. Enzyme Commission Number: EC 5.4.99.2. CAS No. 9023-90-9. 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-5559; methylmalonyl-CoA mutase; EC 5.4.99.2; 9023-90-9; methylmalonyl-CoA CoA-carbonyl mutase; methylmalonyl coenzyme A mutase; methylmalonyl coenzyme A carbonylmutase; (S)-methylmalonyl-CoA mutase; (R)-2-methyl-3-oxopropanoyl-CoA CoA-carbonylmutase [incorrect]. Cat No: EXWM-5559. | |
| Native Baker's yeast (S. cerevisiae) Triosephosphate Isomerase | Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess differential expression of fourteen proteins of uveal melanoma. triosephosphate isomerase has also been used in a study to investigate the use of sigmoid ph gradients in free-flow isoelectric f ocusing of human endothelial cell proteins. Group: Enzymes. Synonyms: Triose-. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: ~10,000 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Crystalline suspension in 2.7 M (NH4)2SO4, 0.5 mM EDTA, pH 6.5. Source: Baker's yeast (S. cerevisiae). Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0711. | |
| Native Chicken Phosphoglucomutase | Phosphoglucomutase (EC 5.4.2.2) is an enzyme that transfers a phosphate group on an α-D-glucose monomer from the 1' to the 6' position in the forward direction or the 6' to the 1' position in the reverse direction. More precisely, it facilitates the interconversion of glucose 1-phosphate and glucose 6-phosphate. Group: Enzymes. Synonyms: EC 5.4.2.2; PGM; phosphoglucomutase; α-D-Glucose-1,6-bisphosphatase, α-D-Glucose-1-phosphate phosphotransferase, Phosphoglucomutase-1, PGM-1, PGM 1, Glucose phosphomutase 1; Glucose phosphomutase; Phosphoglucose mutase. Enzyme Commission Number: EC 5.4.2.2. CAS No. 9001-81-4. Phosphoglucomutase. Activity: > 10 Units / mg. Storage: Below -20°C. Form: Frozen Liquid. Source: Chicken Muscle. Species: Chicken. EC 5.4.2.2; PGM; phosphoglucomutase; α-D-Glucose-1,6-bisphosphatase, α-D-Glucose-1-phosphate phosphotransferase, Phosphoglucomutase-1, PGM-1, PGM 1, Glucose phosphomutase 1; Glucose phosphomutase; Phosphoglucose mutase. Cat No: NATE-1032. | |
| Native Horseradish Superoxide Dismutase | Superoxide dismutases (SOD) are enzymes that alternately catalyze the dismutation (or partitioning) of the superoxide (O2-) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage. Hydrogen peroxide is also damaging, but less so, and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use a different mechanism to prevent damage from reactive (O2-). Applications: Superoxide dism...mutase and glutathione reductase, and environmental and xenobiotic stress tolerance in maize inbreds. superoxide dismutase from horseradish has also been used in a study to investigate chemiluminometric enzyme sensors for flow-injection analysis. Group: Enzymes. Synonyms: EC 1.15.1.1; 9054-89-1; SOD; Superoxide:superoxide oxidoreductase; Superoxide Dismutase. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Activity: 1,000-4,000 units/mg protein. Stability: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Horseradish. EC 1.15.1.1; 9054-89-1; SOD; Superoxide:superoxide oxidoreductase; Superoxide Dismutase. Cat No: NATE-0679. | |
| Native Microbial α-phosphoglucomutase | Phosphoglucomutase (EC 5.4.2.2) is an enzyme that transfers a phosphate group on an α-D-glucose monomer from the 1' to the 6' position in the forward direction or the 6' to the 1' position in the reverse direction. More precisely, it facilitates the interconversion of glucose 1-phosphate and glucose 6-phosphate. High purity recombinant α-phosphoglucomutase (microbial) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Group: Enzymes. Synonyms: α-phosphoglucomutase; Phosphoglucomutase; EC 5.4.2.2; Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent); Glucose phosphomutase; Phosphoglucose mutase. Enzyme Commission Number: EC 5.4.2.2. CAS No. 9001-81-4. Phosphoglucomutase. Mole weight: MW ~ 59.2 kDa. Source: Microbial. α-phosphoglucomutase; Phosphoglucomutase; EC 5.4.2.2; Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent); Glucose phosphomutase; Phosphoglucose mutase. Cat No: DIA-265. | |
| Native Rabbit Phosphoglucomutase | Phosphoglucomutase (EC 5.4.2.2) is an enzyme that transfers a phosphate group on an α-D-glucose monomer from the 1' to the 6' position in the forward direction or the 6' to the 1' position in the reverse direction. More precisely, it facilitates the interconversion of glucose 1-phosphate and glucose 6-phosphate. Group: Enzymes. Synonyms: EC 5.4.2.2; PGM; phosphoglucomutase; α-D-Glucose-1,6-bisphosphatase, α-D-Glucose-1-phosphate phosphotransferase, Phosphoglucomutase-1, PGM-1, PGM 1, Glucose phosphomutase 1; Glucose phosphomutase; Phosphoglucose mutase. Enzyme Commission Number: EC 5.4.2.2. CAS No. 9001-81-4. Purity: Purified. Phosphoglucomutase. Activity: Reported in U/mL. Storage: 2-8°C. Form: Liquid. Source: Rabbit Muscle. Species: Rabbit. EC 5.4.2.2; PGM; phosphoglucomutase; α-D-Glucose-1,6-bisphosphatase, α-D-Glucose-1-phosphate phosphotransferase, Phosphoglucomutase-1, PGM-1, PGM 1, Glucose phosphomutase 1; Glucose phosphomutase; Phosphoglucose mutase. Cat No: NATE-0556. | |
| Native Rabbit Triosephosphate Isomerase | Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess molecular characterizations of cryptosporidium, giardia, and enter ...e phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: Type I, > 4,000 units/mg protein; Type II, > 3,500 units/mg protein. Storage: -20°C. Form: Type I, ammonium sulfate suspension; Crystalline suspension in 3.2 M (NH4)2SO4 solution, pH 6.0; Type II, lyophilized powder, Sulfate-free, contains EDTA and borate buffer salts. Source: Rabbit muscle. Species: Rabbit. Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0712. | |
| Native Saccharomyces cerevisiae Glyoxalase I | Glyoxalase I is universally expressed and involved in the protection against cellular damage due to cytotoxic metabolites such as advanced glycation end products (AGEs). It is an integral component of the detoxification system, catalyzing the conversion of reactive, acyclic a-oxoaldehydes into the corresponding a-hydroxyacids in a glutathione-dependent manner. Glyoxalase detoxification system consists of glyoxalase (glo)-i and glo-ii. glo-i is a cytosolic, 42 kda, dimeric zn2+ metalloenzyme. Group: Enzymes. Synonyms: lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Enzyme Commission Number: EC 4.4.1.5. CAS No. 9033-12-9. Glyoxalase I. Mole weight: 42 kDa. Activity: > 400 units/mg protein. Storage: 2-8°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol, 0.4 M (NH4)2SO4 and 0.002 M KH2PO4 pH 6.5. Source: Saccharomyces cerevisiae. lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Cat No: NATE-0308. | |
| phosphoacetylglucosamine mutase | The enzyme is activated by N-acetyl-α-D-glucosamine 1,6-bisphosphate. Group: Enzymes. Synonyms: acetylglucosamine phosphomutase; acetylglucosamine phosphomutase; acetylaminodeoxyglucose phosphomutase; phospho-N-acetylglucosamine mutase; N-acetyl-D-glucosamine 1,6-phosphomutase. Enzyme Commission Number: EC 5.4.2.3. CAS No. 9027-51-4. 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-5525; phosphoacetylglucosamine mutase; EC 5.4.2.3; 9027-51-4; acetylglucosamine phosphomutase; acetylglucosamine phosphomutase; acetylaminodeoxyglucose phosphomutase; phospho-N-acetylglucosamine mutase; N-acetyl-D-glucosamine 1,6-phosphomutase. Cat No: EXWM-5525. | |
| phosphoenolpyruvate mutase | Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate. Group: Enzymes. Synonyms: phosphoenolpyruvate-phosphonopyruvate phosphomutase; PEP phosphomutase; phosphoenolpyruvate phosphomutase; PEPPM; PEP phosphomutase. Enzyme Commission Number: EC 5.4.2.9. CAS No. 115756-49-5. 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-5531; phosphoenolpyruvate mutase; EC 5.4.2.9; 115756-49-5; phosphoenolpyruvate-phosphonopyruvate phosphomutase; PEP phosphomutase; phosphoenolpyruvate phosphomutase; PEPPM; PEP phosphomutase. Cat No: EXWM-5531. | |
| 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. | |
| phosphoglucosamine mutase | The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. The enzyme from Escherichia coli is activated by phosphorylation and can be autophosphorylated in vitro by α-D-glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, α-D-glucose 1,6-bisphosphate or ATP. It can also catalyse the interconversion of α-D-glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate. Group: Enzymes. Enzyme Commission Number: EC 5.4.2.10. CAS No. 9031-92-9. 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-5521; phosphoglucosamine mutase; EC 5.4.2.10; 9031-92-9. Cat No: EXWM-5521. | |
| Phosphoglycerate mutase 1 from Human, Recombinant | Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase. Group: Enzymes. Synonyms: Pgam-1; PGAM1. Enzyme Commission Number: EC 5.4.2.1. Purity: > 90% by SDS-PAGE. Mole weight: 30.9 kDa. Activity: >300 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli and fused to His-tag at N-terminus. Species: Human. Pgam-1; PGAM1; Phosphoglycerate mutase 1; Phosphoglycerate mutase. Cat No: NATE-1647. | |
| Phosphoglycerate mutase 1 from Mouse, Recombinant | Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase. Group: Enzymes. Synonyms: Pgam-1; PGAM1. Enzyme Commission Number: EC 5.4.2.1. Purity: > 95% by SDS-PAGE. Mole weight: 31.4 kDa. Activity: >150 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli and fused to His-tag at N-terminus. Species: Mouse. Pgam-1; PGAM1; Phosphoglycerate mutase 1; Phosphoglycerate mutase. Cat No: NATE-1646. | |
| phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) | The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reacti... dPGM. Enzyme Commission Number: EC 5.4.2.11. 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-5522; phosphoglycerate mutase (2,3-diphosphoglycerate-dependent); EC 5.4.2.11; glycerate phosphomutase (diphosphoglycerate cofactor); 2,3-diphosphoglycerate dependent phosphoglycerate mutase; cofactor dependent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); MPGM; PGAM; PGAM-d; PGM; dPGM. Cat No: EXWM-5522. | |
| phosphoglycerate mutase (2,3-diphosphoglycerate-independent) | The enzymes from higher plants, algae, fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction. Group: Enzymes. Synonyms: cofactor independent phosphoglycerate mutase; 2,3-diphosphoglycerate-independent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); pho. Enzyme Commission Number: EC 5.4.2.12. 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-5523; phosphoglycerate mutase (2,3-diphosphoglycerate-independent); EC 5.4.2.12; cofactor independent phosphoglycerate mutase; 2,3-diphosphoglycerate-independent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); iPGM; iPGAM; PGAM-i. Cat No: EXWM-5523. | |
| Phosphoglycerate mutase 2 from Human, Recombinant | Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase. Group: Enzymes. Synonyms: GSD10; PGAM-M; PGAMM; PGAM2. Enzyme Commission Number: EC 5.4.2.11. Purity: > 95% by SDS-PAGE. Mole weight: 30.9 kDa. Activity: >100 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli and fused to His-tag at N-terminus. Species: Human. GSD10; PGAM-M; PGAMM; PGAM2; Phosphoglycerate mutase 2; Phosphoglycerate mutase. Cat No: NATE-1643. | |
| phosphomannomutase | α-D-Mannose 1,6-bisphosphate or α-D-glucose 1,6-bisphosphate can act as cofactor. Group: Enzymes. Synonyms: mannose phosphomutase; phosphomannose mutase; D-mannose 1,6-phosphomutase. Enzyme Commission Number: EC 5.4.2.8. CAS No. 59536-73-1. 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-5530; phosphomannomutase; EC 5.4.2.8; 59536-73-1; mannose phosphomutase; phosphomannose mutase; D-mannose 1,6-phosphomutase. Cat No: EXWM-5530. | |
| 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. | |
| phosphonopyruvate hydrolase | Highly specific for phosphonopyruvate as substrate. The reaction is not inhibited by phosphate but is inhibited by the phosphonates phosphonoformic acid, hydroxymethylphosphonic acid and 3-phosphonopropanoic acid. The enzyme is activated by the divalent cations Co2+, Mg2+ and Mn2+. This enzyme is a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily. Group: Enzymes. Synonyms: PPH. Enzyme Commission Number: EC 3.11.1.3. 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-3776; phosphonopyruvate hydrolase; EC 3.11.1.3; PPH. Cat No: EXWM-3776. | |
| phosphoribosylaminoimidazole carboxylase | While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, namely EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase and EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase. 5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate. Group: Enzymes. Synonyms: 5-phosphoribosyl-5-aminoimidazole carboxylase; 5-amino-1-ribosylimidazole 5-phosphate carboxylase; AIR carboxylase; 1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase; ADE2; class II PurE; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase. Enzyme Commission Number: EC 4.1.1.21. CAS No. 9032-4-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4766; phosphoribosylaminoimidazole carboxylase; EC 4.1.1.21; 9032-04-6; 5-phosphoribosyl-5-aminoimidazole carboxylase; 5-amino-1-ribosylimidazole 5-phosphate carboxylase; AIR carboxylase; 1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase; ADE2; class II PurE; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase. Cat No: EXWM-4766. | |
| prephenate dehydratase | This enzyme in the enteric bacteria also possesses chorismate mutase (EC 5.4.99.5) activity, and converts chorismate into prephenate. Group: Enzymes. Synonyms: prephenate hydro-lyase (decarboxylating). Enzyme Commission Number: EC 4.2.1.51. CAS No. 9044-88-6. 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-5041; prephenate dehydratase; EC 4.2.1.51; 9044-88-6; prephenate hydro-lyase (decarboxylating). Cat No: EXWM-5041. | |
| prephenate dehydrogenase | This enzyme in the enteric bacteria also possesses chorismate mutase activity (EC 5.4.99.5 chorismate mutase) and converts chorismate into prephenate. Group: Enzymes. Synonyms: hydroxyphenylpyruvate synthase; chorismate mutase-prephenate dehydrogenase. Enzyme Commission Number: EC 1.3.1.12. CAS No. 9044-92-2. 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-1286; prephenate dehydrogenase; EC 1.3.1.12; 9044-92-2; hydroxyphenylpyruvate synthase; chorismate mutase-prephenate dehydrogenase. Cat No: EXWM-1286. | |
| protostadienol synthase | (17Z)-Protosta-17(20),24-dien-3β-ol is a precursor of the steroidal antibiotic helvolic acid. Group: Enzymes. Synonyms: PdsA; (S)-2,3-epoxysqualene mutase [cyclizing, (17Z)-protosta-17(20),24-dien-3β-ol-forming]. Enzyme Commission Number: EC 5.4.99.32. 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-5573; protostadienol synthase; EC 5.4.99.32; PdsA; (S)-2,3-epoxysqualene mutase [cyclizing, (17Z)-protosta-17(20),24-dien-3β-ol-forming]. Cat No: EXWM-5573. | |
| taraxerol synthase | The enzyme gives taraxerol, β-amyrin and lupeol in the ratio 70:17:13. Group: Enzymes. Synonyms: RsM2; (S)-2,3-epoxysqualene mutase (cyclizing, taraxerol-forming). Enzyme Commission Number: EC 5.4.99.35. 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-5576; taraxerol synthase; EC 5.4.99.35; RsM2; (S)-2,3-epoxysqualene mutase (cyclizing, taraxerol-forming). Cat No: EXWM-5576. | |
| thalianol synthase | This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. Group: Enzymes. Synonyms: (S)-2,3-epoxysqualene mutase (cyclizing, thalianol-forming). Enzyme Commission Number: EC 5.4.99.31. 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-5572; thalianol synthase; EC 5.4.99.31; (S)-2,3-epoxysqualene mutase (cyclizing, thalianol-forming). Cat No: EXWM-5572. | |
| triose-phosphate isomerase | Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. Group: Enzymes. Synonyms: phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. 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-5452; triose-phosphate isomerase; EC 5.3.1.1; 9023-78-3; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase. Cat No: EXWM-5452. | |
| tRNA pseudouridine55 synthase | Pseudouridine synthase TruB from Escherichia coli specifically modifies uridine55 in tRNA molecules. The bifunctional archaeal enzyme also catalyses the pseudouridylation of uridine54. It is not known whether the enzyme from Escherichia coli can also act on position 54 in vitro, since this position is occupied in Escherichia coli tRNAs by thymine. Group: Enzymes. Synonyms: TruB; aCbf5; Pus4; YNL292w (gene name); ψ55 tRNA pseudouridine synthase; tRNA:ψ55-synthase; tRNA pseudouridine 55 synthase; tRNA:pseudouridine-55 synthase; ψ55 synthase; tRNA ψ55 synthase; tRNA:ψ55 synthase; tRNA-uridine55 uracil mutase; Pus10; tRNA-uridine54/55 uracil mutase. Enzyme Commission Number: EC 5.4.99.25. CAS No. 430429-15-5. 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-5565; tRNA pseudouridine55 synthase; EC 5.4.99.25; 430429-15-5; TruB; aCbf5; Pus4; YNL292w (gene name); ψ55 tRNA pseudouridine synthase; tRNA:ψ55-synthase; tRNA pseudouridine 55 synthase; tRNA:pseudouridine-55 synthase; ψ55 synthase; tRNA ψ55 synthase; tRNA:ψ55 synthase; tRNA-uridine55 uracil mutase; Pus10; tRNA-uridine54/55 uracil mutase. Cat No: EXWM-5565. | |
| tyrosine 2,3-aminomutase | Requires ATP. Group: Enzymes. Synonyms: tyrosine α,β-mutase. Enzyme Commission Number: EC 5.4.3.6. CAS No. 9073-38-5. 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-5538; tyrosine 2,3-aminomutase; EC 5.4.3.6; 9073-38-5; tyrosine α,β-mutase. Cat No: EXWM-5538. | |
| UDP-arabinopyranose mutase | The reaction is reversible and at thermodynamic equilibrium the pyranose form is favored over the furanose form (90:10). Group: Enzymes. Synonyms: Os03g40270 protein; UAM1; UAM3; RGP1; RGP3; OsUAM1; OsUAM2; Os03g0599800 protein; Os07g41360 protein. Enzyme Commission Number: EC 5.4.99.30. 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-5571; UDP-arabinopyranose mutase; EC 5.4.99.30; Os03g40270 protein; UAM1; UAM3; RGP1; RGP3; OsUAM1; OsUAM2; Os03g0599800 protein; Os07g41360 protein. Cat No: EXWM-5571. | |
| UDP-galactopyranose mutase | A flavoenzyme which generates UDP-α-D-glactofuranose required for cell wall formation in bacteria, fungi, and protozoa. Group: Enzymes. Synonyms: UGM; UDP-D-galactopyranose furanomutase. Enzyme Commission Number: EC 5.4.99.9. CAS No. 174632-18-9. 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-5609; UDP-galactopyranose mutase; EC 5.4.99.9; 174632-18-9; UGM; UDP-D-galactopyranose furanomutase. Cat No: EXWM-5609. | |
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