Kidney glycine oxidase

Early studies performed with bovine plasma and porcine kidney amine oxidases have shown that the enzymes undergo irreversible inactivation upon reaction with several acetylenic substrates (propargylamine, 2-chloroallylamine and 2-butyne-1,4-diamine), which was diminished by substrate protection [118]. Other types of mechanism-based inactivators of bovine plasma amine oxidase are some glycine esters with relatively acidic a-protons. These esters are converted to ketenes, which may acylate the active site and inactivate the enzyme [119]. 

They exist with relatively low activity in peroxisomes in the liver and kidney. The most important D-amino acid oxidase is glycine oxidase, an FAD-containing enzyme that catalyzes the formation of glyoxylate and also acts on D-amino acids to form their corresponding 2-oxoacid. Glyoxylate is further oxidized to COj and formate, HCOO , which is used in one-carbon (Cl) metabolism. 

Glycine is converted to glyoxylic acid by two different pathways oxidation and transamination. Glycine oxidase, an enzyme found in liver and kidney, deami-... 

Glycine oxidase has been found in the liver or kidney of all animals tested, and is a flavoprotein which can be resolved under acid conditions into a protein and FAD. 

Glyoxylate could be formed from glycine mther by the action of glycine oxidase SS) or by transamination SS, 34). Glycine oxidase is a flavoprotein that has been found in liver and kidney. Because of its comparatively high Km value (0.04 M) and its low turnover number it generally is considered not to have any considerable role in the metabolism of gl3rcine. 

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