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Phenylalanine hydroxylase (PAH) (EC 1.14.16.1) is an enzyme that catalyses the reaction responsible for the addition of a hydroxyl group to the end of the 6-carbon aromatic ring of phenylalanine, such that it becomes tyrosine.
Polyvinyl-alcohol oxidase is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor.It is produced from Pseudomonas species strain VM15C.
Thiosulfate dehydrogenase (EC 1.8.2.2) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a cytochrome as acceptor. The systematic name of this enzyme class is thiosulfate:ferricytochrome-c oxidoreductase.
Vellosimine dehydrogenase (EC 1.1.1.273) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 10-deoxysarpagine:NADP+ oxidoreductase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
Propionyl-CoA carboxylase catalyses the carboxylation reaction of propionyl CoA. The enzyme is biotin dependent.Propionyl CoA is the end product of metabolism of odd-chain fatty acids, and is also a metabolite of most methyl-branched fatty acids. It is also the main metabolite of valine, and together with acetyl-CoA, is a metabolite of isoleucine, as well as a methionine metabolite.
pyridoxal 4-dehydrogenase (EC 1.1.1.107) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is pyridoxal:NAD+ 4-oxidoreductase. This enzyme is also called pyridoxal dehydrogenase. This enzyme participates in vitamin B6 metabolism.
Acetaldehyde dehydrogenases (EC 1.2.1.10) are dehydrogenase enzymes which catalyze the conversion of acetaldehyde into acetic acid.
Acetoacetate decarboxylase (ADC) is an enzyme involved in both the ketone body production pathway in humans and other mammals, and solventogenesis in certain bacteria. Its reaction involves a decarboxylation of acetoacetate, forming acetone and carbon dioxide. The enzyme works in the cytosol of cells and demonstrates a maximum activity at pH 5.95. In humans and other mammals, this reaction can take place spontaneously, or through the catalytic actions of acetoacetate decarboxylase.
Acetolactate Decarboxylase is belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase [(R)-2-acetoin-forming].This enzyme participates in butanoate metabolism and c5-branched dibasic acid metabolism. Acetolactate Decarboxylase is an enzyme that is a processing aid when low-enzyme malt is used. It lowers the cost because less malt is required and provides for faster fermentation. It is used in beer.
Adenylyl-sulfate reductase (glutathione) (EC 1.8.4.9) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is AMP,sulfite:glutathione-disulfide oxidoreductase.
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