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| Product | Description | |
|---|---|---|
| cypemycin cysteine dehydrogenase (decarboxylating) | Cypemycin, isolated from the bacterium Streptomyces sp. OH-4156, is a peptide antibiotic, member of the linaridins, a class of posttranslationally modified ribosomally synthesized peptides. The enzyme decarboxylates and reduces the C-terminal L-cysteine residue, producing a reactive ethenethiol group that reacts with a dethiolated cysteine upstream to form an aminovinyl-methyl-cysteine loop that is important for the antibiotic activity of the mature peptide. Group: Enzymes. Synonyms: cypemycin decarboxylase; CypD. Enzyme Commission Number: EC 1.3.99.36. 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-1436; cypemycin cysteine dehydrogenase (decarboxylating); EC 1.3.99.36; cypemycin decarboxylase; CypD. Cat No: EXWM-1436. |  |
| Alanine Dehydrogenase from Bacillus cereus, Recombinant | L-Alanine dehydrogenase is an A-stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the geneRation of pyruvate during sporulation. L-Alanine dehydrogenase from Bacillus subtilis has a predominately ordered kinetic mechanism in which NAD binds before L-alanine. Subsequently, ammonia, pyruvate, and NADH are released in that specific order. Optimal pH for the amination reaction is 8.8-9.0, whereas it is 10-10.5 for the deamination reaction. The enzyme is inactivated by divalent metal ions and p-chloromercuribenzoate, mercuric ion being most effective. The inactivation may be reversed by L-or D-cysteine. Group: Enzymes. Synonyms: L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alan. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: > 350 units/ml. Storage: -20°C. Source: E. coli. Species: Bacillus cereus. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-0044. | |
| alanopine dehydrogenase | In the reverse reaction, L-alanine can be replaced by L-cysteine, L-serine or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22 strombine dehydrogenase). Group: Enzymes. Synonyms: ALPDH alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase; meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase; alanopine: NAD oxidoreductase; ADH; alanopine:NAD oxidoreductase. Enzyme Commission Number: EC 1.5.1.17. CAS No. 71343-07-2. 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-1498; alanopine dehydrogenase; EC 1.5.1.17; 71343-07-2; ALPDH alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase; meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase; alanopine: NAD oxidoreductase; ADH; alanopine:NAD oxidoreductase. Cat No: EXWM-1498. | |
| Heptelidic acid | It is produced by the strain of Gliocladium virens, Chaetomium globosum, Trichoderma viride. It is a sesquiterpenoid antibiotic. It has antibacterial activity against anaerobes, especially has strong effect on fragile bacilli (MIC is 0.4 μg/mL). It has anti-plasmodium (IC80 is 0.01 μg/mL) and antitumor activity. It is also an inhibitor of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) that acts by binding to the cysteine-149 residue. Synonyms: Koningic acid; (+)-Heptelidic Acid; (5aS,6R,9S,9aS)-6-isopropyl-1-oxo-1,5a,6,7,8,9a-hexahydro-3H-spiro[benzo[c]oxepine-9,2'-oxirane]-4-carboxylic acid; Spiro[2-benzoxepin-9(3H),2'-oxirane]-4-carboxylicacid,1,5a,6,7,8,9a-hexahydro-6-(1-methylethyl)-1-oxo-, (2'S,5aS,6R,9aS)-; Avocettin. Grades: ≥95%. CAS No. 57710-57-3. Molecular formula: C15H20O5. Mole weight: 280.32. |  |
| JX-06 | JX-06 is a potent and selective pyruvate dehydrogenase kinase (PDK) 1/2/3 inhibitor (IC50 values are 28, 49 and 313 nM for PDK2, PDK1 and PDK3, respectively). JX06 Selectively Inhibits Pyruvate Dehydrogenase Kinase PDK1 by a Covalent Cysteine Modification. JX06, as a selective covalent inhibitor of PDK1 in cells, forms a disulfide bond with the thiol group of a conserved cysteine residue (C240) based on recognition of a hydrophobic pocket adjacent to the ATP pocket of the PDK1 enzyme. Group: Inhibitors. Alternative Names: JX-06; JX 06; JX06. CAS No. 729-46-4. Molecular formula: C10H16N2O2S4. Mole weight: 324.49. Appearance: Solid powder. Purity: >98%. IUPACName: Bis(morpholinothiocarbonyl) disulfide. Canonical SMILES: S=C(SSC(N1CCOCC1)=S)N2CCOCC2. Catalog: ACM729464. |  |
| lysine 6-dehydrogenase | The enzyme is highly specific for L-lysine as substrate, although S-(2-aminoethyl)-L-cysteine can act as a substrate, but more slowly. While the enzyme from Agrobacterium tumefaciens can use only NAD+, that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP+, but more slowly. Group: Enzymes. Synonyms: L-lysine ε-dehydrogenase; L-lysine 6-dehydrogenase; LysDH. Enzyme Commission Number: EC 1.4.1.18. CAS No. 89400-30-6. 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-1451; lysine 6-dehydrogenase; EC 1.4.1.18; 89400-30-6; L-lysine ε-dehydrogenase; L-lysine 6-dehydrogenase; LysDH. Cat No: EXWM-1451. | |
| thiomorpholine-carboxylate dehydrogenase | The product is the cyclic imine of the 2-oxoacid corresponding to S-(2-aminoethyl)cysteine. In the reverse direction, a number of other cyclic unsaturated compounds can act as substrates, but more slowly. Group: Enzymes. Synonyms: ketimine reductase; ketimine-reducing enzyme. Enzyme Commission Number: EC 1.5.1.25. CAS No. 115232-54-7. 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-1507; thiomorpholine-carboxylate dehydrogenase; EC 1.5.1.25; 115232-54-7; ketimine reductase; ketimine-reducing enzyme. Cat No: EXWM-1507. | |
| xanthine dehydrogenase | Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Enzyme Commission Number: EC 1.17.1.4. CAS No. 9054-84-6. XDH. 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-1082; xanthine dehydrogenase; EC 1.17.1.4; 9054-84-6; NAD+-xanthine dehydrogenase; xanthine-NAD+ oxidoreductase; xanthine/NAD+ oxidoreductase; xanthine oxidoreductase. Cat No: EXWM-1082. | |
| xanthine oxidase | An iron-molybdenum flavoprotein (FAD) containing [2Fe-2S] centres. Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1, aldehyde oxidase. Under some conditions the product is mainly superoxide rather than peroxide: RH + H2O + 2 O2 = ROH + 2 O2.- + 2 H+. The mammalian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4, xanthine dehydrogenase). During purification the enzyme is largely converted to the O2-dependent xanthine oxidase form (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo. Group: Enzymes. Synonyms: hypoxanthine o. Enzyme Commission Number: EC 1.17.3.2. CAS No. 9002-17-9. 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-1088; xanthine oxidase; EC 1.17.3.2; 9002-17-9; hypoxanthine oxidase; hypoxanthine:oxygen oxidoreductase; Schardinger enzyme; xanthine oxidoreductase; hypoxanthine-xanthine oxidase; xanthine:O2 oxidoreductase; xanthine:xanthine oxidase. Cat No: EXWM-1088. | |
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