Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
33551 | New Biotechnology | 2010 | 4 Pages |
The present paper reviews the enzymes catalyzing conversion of Nα-benzyloxycarbonyl-l-lysine (Nα-Z-l-lysine) to Nα-benzyloxycarbonyl-l-aminoadipic acid (Nα-Z-l-AAA) in fungal and bacterial strains. Aspergillus niger AKU 3302 and Rhodococcus sp. AIU Z-35-1 converted Nα-Z-l-lysine to Nα-Z-l-AAA via Nα-benzyloxycarbonyl-l-aminoadipate-δ-semialdehyde (Nα-Z-l-AASA). However, different enzyme combinations were involved in the Nα-Z-l-lysine metabolism of both strains. A. niger strain converted Nα-Z-l-lysine to Nα-Z-l-AASA by amine oxidase, and the resulting Nα-Z-l-AASA was converted to Nα-Z-l-AAA by an aldehyde oxidase. In the Rhodococcus strain, conversion of Nα-Z-l-lysine to Nα-Z-l-AASA was catalyzed by l-specific amino acid oxidase. The resulting Nα-Z-l-AASA was converted to Nα-Z-l-AAA by an aldehyde dehydrogenase. The present paper also describes characteristics of new enzymes obtained from those strains.