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LAAOL-Amino Acid Oxidase (enzyme)
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References in periodicals archive ?
In Vitro Determination of Essential Oils Effect on L-Amino Acid Oxidase Activity
A spectrophotometric microplate assay for L-amino acid oxidase.
Escapin is an L-amino acid oxidase that oxidizes its substrates, L-lysine and L-arginine in opaline, when ink and opaline are secreted simultaneously, and produces a complex set of compounds that are mild deterrents against Panulirus interruptus and Callinectes sapidus (Yang et al.
Defense through chemoreception: an L-amino acid oxidase in the ink of sea hares deters predators through their chemical senses.
The chemistry of escapin: identification and quantification of the components in the complex mixture generated by an L-amino acid oxidase in the defensive secretion of the sea snail Aplysia californica.
An example is the products of the oxidation of L-lysine (present in high doses in opaline) by escapin (an L-amino acid oxidase that is present only in ink), which are produced only when ink and opaline are co-secreted and mixed in the mantle cavity just prior to release (Kicklighter et al.
Cloning and biochemical characterization of APIT, a new L-amino acid oxidase from Aplysia punctata.
L-Amino acid oxidase activity of an antineoplastic factor of a marine mollusk and its relationship to cytotoxicity.
Snake venom protein (such as phospholipase A2 metalloproteinases serinoproteases L-amino acid oxidases lectin and other) and peptides (brady kinin potentiators analgesic peptides and other) have found practical application as pharmaceutical agents with significant therapeutic values.
L-amino acid oxidases (LAOX) catalyse the stereospecific oxidative deamination of amino acid substrates to the corresponding a-keto acids along with the production of ammonia and hydrogen peroxide via an imino acid intermediate [2].