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In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction choline + O2↔ betaine aldehyde + H2O2. Thus, the two substrates of this enzyme are choline and O2, whereas its two products are betaine aldehyde and H2O2.http://www.creative-enzymes.com/product/Native-Arthrobacter-Globiformis-Choline-Oxidase_735.html
This enzyme is more active at a higher pH range than the known alkaline protease, showing the proteolytic activity even in 0.2N NaOH solution. This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein.http://www.creative-enzymes.com/product/Native-Streptomyces-Sp-Alkalophilic-Proteinase_779.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/Native-Bacillus-Subtilis-LAlanine-Dehydrogenase_1246.html
In enzymology, an arginine decarboxylase (EC 4.1.1.19) is an enzyme that catalyzes the chemical reaction:L-arginine↔ agmatine + CO2. Hence, this enzyme has one substRate, L-arginine, and two products, agmatine and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. It employs one cofactor, pyridoxal phosphate.http://www.creative-enzymes.com/product/Native-Escherichia-Coli-LArginine-Decarboxylase_1251.html
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