L-Amino Acid Oxidase from Crotalus adamanteus has been used in the quantification of rid protein in imine deaminase activity.
L-amino acid oxidase (LAAO) is used to convert L-amino acids to their corresponding α-keto acids. L-amino acid oxidase, from Sigma, has been used in leucine aminopeptidase (LAP) activity assays. 35S dimethylsulfoniopropionate (DMSP) has been synthesized chemically from 35S L-methionine using LAAO from Sigma to form 35S 3-methiolpropionate.
L-Amino acid oxidase (LAAO) is a flavoprotein with a molecular weight of 130 kDa. It consists of two different subunits of approximately 70 kDa. Each molecule of holoenzyme has two flavin adenine dinucleotide (FAD) molecules. LAAO is a glycoprotein containing about 2-5% carbohydrate, including sialic acid. optimum pH is approximately 7.5. It occurs in many snake venoms apart from microorganisms and animal tissue, especially in kidney. In the N-terminal region, it has a βαβ domain with glutamic acid residues. LAAO imparts yellow color to venom.
L-Amino acid oxidase is a flavoprotein with a molecular weight of 130 kDa. It consists of two different subunits of approximately 70,000 Da. Each molecule of holoenzyme has two FAD molecules. It is a glycoprotein containing about 2-5% carbohydrate, including sialic acid. Optimum pH is approximately 7.5.The enzyme may be reversibly inactivated by incubation in phosphate buffer, pH 7.5 at 38 °C. L-amino acid oxidase is involved in various metabolic pathways such as alanine and aspartate metabolism, methionine metabolism, valine, leucine and isoleucine degradation, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and alkaloid biosynthesis. It occurs in many snake venoms apart from microorganisms and animal tissue, especially in kidney and liver.
