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.
Isobe
Kimiyasu
K
Department of Agro-bioscience, Faculty of Agriculture, Iwate University, 3 Ueda, Morioka 020-8550, Japan. kiso@iwate-u.ac.jp
Ishikura
Kazuna
K
Shimizu
Sakayu
S
D015074:2-Aminoadipic Acid / Q000737:chemistry; D000438:Alcohols / Q000737:chemistry; D042931:Aldehyde Oxidase / Q000737:chemistry; D000447:Aldehydes / Q000737:chemistry; D000588:Amines / Q000737:chemistry; D001234:Aspergillus niger / Q000378:metabolism*; D002384:Catalysis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008956:Models, Chemical; D010088:Oxidoreductases / Q000737:chemistry; D013379:Substrate Specificity; D013696:Temperature; D013997:Time Factors
D000438:Alcohols; D000447:Aldehydes; D000588:Amines; D015074:2-Aminoadipic Acid; D010088:Oxidoreductases; D042931:Aldehyde Oxidase