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Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.http://www.creative-enzymes.com/product/3AcetylpyridineAdenine-Dinucleotide-Reduced-APADH-_1508.html
Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is an cytosolic enzyme that catalyzes the chemical reaction: D-glucose 6-phosphate + NADP+↔ 6-phospho-D-glucono-1, 5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway (see image), a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH).http://www.creative-enzymes.com/product/Native-Microorganism-Glucose6phosphate-Dehydrogenase_741.html
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.http://www.creative-enzymes.com/product/Alanine-Dehydrogenase-From-Bacillus-Cereus-Recombinant_1712.html
In enzymology, a protocatechuate 3,4-dioxygenase (EC 1.13.11.3) is an enzyme that catalyzes the chemical reaction: 3,4-dihydroxybenzoate + O2 ↔ 3-carboxy-cis,cis-muconate. Thus, the two substrates of this enzyme are 3,4-dihydroxybenzoate (protocatechuic acid) and O2, whereas its product is 3-carboxy-cis,cis-muconate. This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, iron.http://www.creative-enzymes.com/product/Native-Pseudomonas-Sp-Protocatechuate-3-4dioxygenase_810.html
Prolyl endopeptidase (PE) also known as prolyl oligopeptidase or post-proline cleaving enzyme is an enzyme that in humans is encoded by the PREP gene.http://www.creative-enzymes.com/product/Native-Flavobacterium-Sp-Proline-Specific-Endopeptidase_809.html
In enzymology, a 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) is an enzyme that catalyzes the chemical reaction: (R)-3-hydroxybutanoate + NAD+ ↔ acetoacetate + NADH + H+. Thus, the two substrates of this enzyme are (R)-3-hydroxybutanoate and NAD+, whereas its three products are acetoacetate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in synthesis and degradation of ketone bodies and butanoate metabolism.http://www.creative-enzymes.com/product/Native-Pseudomonas-Sp-D3hydroxybutyrate-Dehydrogenase_800.html
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