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Enzymatic Cascade Reactions for the Synthesis of Chiral Amino Alcohols from L-lysine
Published on: February 16, 2018
Enzymes responsible for metabolism of Nα-benzyloxycarbonyl-L-lysine in microorganisms
1Department of Biological Chemistry and Food Science, Iwate University, Morioka 020-8550, Japan. kiso@iwate-u.ac.jp
Abstract:
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.
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