Identification and Characterization of Enzyme Catalyzing Conversion of N^α-Benzyloxycarbonyl-L-Aminoadipic-δ-Semialdehyde to N^α-Benzyloxycarbonyl-L-Aminoadipic Acid in Aspergillus niger AKU 3302(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)

概要

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The enzyme catalyzing the conversion of N^α-benzyloxycarbonyl-L-aminoadipic-δ-semialdehyde (N^α-Z-L-AASA) to N^α-benzyloxycarbonyl-L-aminoadipic acid (N^α-Z-L-AAA) in Aspergillus niger AKU 3302 was identified, and its characteristics were revealed. This reaction was catalyzed by an oxidase with a molecular mass of 215 kDa and pI of 4.1. The enzyme exhibited oxidase activity on N^α-Z-L-AASA but not on short-chain aliphatic aldehydes, aromatic aldehydes or alcohols. The apparent K_m value for N^α-Z-L-AASA was estimated to be 7.0mM. Thus, N^α-Z-L-lysine was converted to N^α-Z-L-AAA via N^α-Z-L-AASA by a combination of an amine oxidase with broad substrate specificity and an aldehyde oxidase specific to N^α-Z-L-AASA in A. niger AKU 3302.
社団法人日本生物工学会の論文
2008-10-25