Chemistry & Biodiversity 2010-06-01

Enzymes responsible for the conversion of N alpha-[(Benzyloxy)carbonyl]-D-lysine to N alpha-[(Benzyloxy)carbonyl]-D-aminoadipic acid by Rhodococcus sp. AIU Z-35-1.

Kimiyasu Isobe, Nahoko Fukuda, Shouko Nagasawa, Kaoru Saitou

Index: Chem. Biodivers. 7(6) , 1549-54, (2010)

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Abstract

The enzymes responsible for the conversion of N(alpha)-[(benzyloxy)carbonyl]-D-lysine (N(alpha)-Z-D-lysine) to N(alpha)-Z-D-aminoadipic acid (N(alpha)-Z-D-AAA) by Rhodococcus sp. AIU Z-35-1 were identified. N(alpha)-Z-D-Lysine was first converted to N(alpha)-Z-D-aminoadipic delta-semialdehyde (N(alpha)-Z-D-AASA) by D-specific amino acid deaminase, whereas N(alpha)-Z-L-lysine was converted to N(alpha)-Z-L-AASA by L-specific amino acid oxidase. The resulting N(alpha)-Z-D-AASA was then converted to N(alpha)-Z-D-AAA by the same aldehyde dehydrogenase that is responsible for N(alpha)-Z-L-AASA oxidation. The product amount of the D-specific amino acid deaminase reached the maximum at one day of cultivation in the L-lysine medium. The aldehyde dehydrogenase reached the maximum at three days of cultivation.