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Identification and characterization of enzyme catalyzing conversion of N(alpha)-benzyloxycarbonyl-L-aminoadipic-delta-semialdehyde to N(alpha)-benzyloxycarbonyl-L-aminoadipic acid in Aspergillus niger AKU 3302.

The enzyme catalyzing the conversion of N(alpha)-benzyloxycarbonyl-L-aminoadipic-delta-semialdehyde (N(alpha)-Z-l-AASA) to N(alpha)-benzyloxycarbonyl-L-aminoadipic acid (N(alpha)-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(alpha)-Z-L-AASA but not on short-chain aliphatic aldehydes, aromatic aldehydes or alcohols. The apparent K(m) value for N(alpha)-Z-L-AASA was estimated to be 7.0 mM. Thus, N(alpha)-Z-L-lysine was converted to N(alpha)-Z-L-AAA via N(alpha)-Z-L-AASA by a combination of an amine oxidase with broad substrate specificity and an aldehyde oxidase specific to N(alpha)-Z-L-AASA in A. niger AKU 3302.