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diagnosis, or treatment. Use of this site constitutes acceptance of our User Agreement and Privacy Policy. Learn more.L-Amino acid oxidase
L-amino acid oxidase (LAAO) (EC 1.4.3.3) is an enzyme involved in the metabolism of the polyamines putrescine, spermidine, and spermine. It catalyzes the deamination of L-amino acids to produce the corresponding α-keto acid and ammonia. LAAO is a cytochrome P450 enzyme that is not an electron-transport chain component of the electron transport chain but acts in a strictly dehydrogenase-like manner in oxidizing substrates. LAAO is expressed in the venom of a wide variety of animals, including snakes, frogs, lizards, and marine animals.
Enzymology
LAAO has a wide substrate range, and as such is not highly specific. While the L- and D-isomers of most naturally occurring amino acids are oxidized by LAAO, this enzyme prefers L-amino acids over D-amino acids. LAAO accepts an aromatic ring as part of the substrate as well as the side chains of arginine, lysine, and cysteine.
The reaction catalyzed by LAAO follows a two-step mechanism with release of two hydrogen atoms. In the first step, an iminium ion is formed from the amino acid and cofactor. The iminium ion then undergoes a nucleophilic attack from oxygen to form an imine-hydroperoxide intermediate. The imine-hydroperoxide intermediate is then oxidized to the imine anion, which leaves as ammonia and the α-keto acid. ac619d1d87
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