L-Amino Acid Oxidase from Crotalus adamanteus

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. The enzyme has been immobilized and used in an enzymatic flow-injection procedure with chemiluminescence detection for on-site determination of L-alanine.

L-Amino acid oxidase (LAAO) from Crotalus adamanteus requires Mg²⁺ for its activation. The N-terminal region is essential for FAD binding. The H₂O₂ generated by LAAO based oxidation reactions lead to prevention of platelet aggregation and induces edema and apoptosis. LAAO activity is inhibited by ethylenediaminetetraacetic acid (EDTA) and phenylmethylsulfonyl fluoride (PMSF).

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.

Dissolves in water at 1 mg/mL concentration to form a clear solution.