Characterization of N^α-Benzyloxycarbonyl-L-Lysine Oxidizing Enzyme from Rhodococcus sp. AIU Z-35-1(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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An oxidase catalyzing conversion of N^α-benzyloxycarbonyl-L-lysine (N^α-Z-L-lysine) to N^α-benzyloxycarbonyl-L-aminoadipate-δ-semialdehyde (N^α-Z-L-AASA) was purified from Rhodococcus sp. AIU Z-35-1, and its properties were revealed. This enzyme catalyzed an oxidative deamination of the ε-amino group of N^α-acyl-L-lysine and the a-amino group of N^ε-acyl-L-lysine. The apparent K_m value for N^α-acetyl-L-lysine was much larger than that for N^ε-acetyl-L-lysine. The peptidyl L-lysines, L-lysine and many other L-amino acids were also oxidized, but N^α-acyl-D-lysine, N^ε-acyl-D-lysine and D-amino acids were not. Thus, the conversion of N^α-Z-L-lysine into N^α-Z-L-AASA was catalyzed by the L-amino acid oxidase with broad substrate specificity. This enzyme, a flavoprotein with a molecular mass of 100 kDa, consisted of two identical subunits of 51 kDa.
2007-09-25