Identification and Characterization of Enzyme Catalyzing Conversion of Nα-Benzyloxycarbonyl-l-Aminoadipic-δ-Semialdehyde to Nα-Benzyloxycarbonyl-l-Aminoadipic Acid in Aspergillus niger AKU 3302
The enzyme catalyzing the conversion of Nα-benzyloxycarbonyl-l-aminoadipic-δ-semialdehyde (Nα-Z-l-AASA) to Nα-benzyloxycarbonyl-l-aminoadipic acid (Nα-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 Nα-Z-l-AASA but not on short-chain aliphatic aldehydes, aromatic aldehydes or alcohols. The apparent Km value for Nα-Z-l-AASA was estimated to be 7.0 mM. Thus, Nα-Z-l-lysine was converted to Nα-Z-l-AAA via Nα-Z-l-AASA by a combination of an amine oxidase with broad substrate specificity and an aldehyde oxidase specific to Nα-Z-l-AASA in A. niger AKU 3302.
Journal: Journal of Bioscience and Bioengineering - Volume 106, Issue 4, October 2008, Pages 409–411