L-Amino acid oxidase as biocatalyst: a dream too far?

摘要: l-Amino acid oxidase (LAAO) is a flavoenzyme containing non-covalently bound flavin adenine dinucleotide, which catalyzes the stereospecific oxidative deamination of l-amino acids to α-keto and also produces ammonia hydrogen peroxide via an imino intermediate. LAAOs purified from snake venoms are best-studied members this family enzymes, although number bacterial fungal sources have been reported. From biochemical point view, different distinguished by molecular mass, substrate specificity, post-translational modifications regulation. In analogy well-known biotechnological applications d-amino oxidase, important results expected availability suitable LAAOs; however, these expectations not fulfilled yet because none “true” has successfully expressed as recombinant protein in prokaryotic hosts, such Escherichia coli. enzyme biotechnology, production mandatory both for large amounts catalyst improve its properties engineering. As alternative, flavoenzymes active on specific identified, e.g., l-aspartate l-lysine l-phenylalanine etc. According presently available information, amino oxidases with “narrow” or “strict” specificity represent good candidates obtain more enlarging their means