Enzymes responsible for metabolism of Nα-benzyloxycarbonyl-L-lysine in microorganisms.
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.
Isobe
Kimiyasu
K
Department of Biological Chemistry and Food Science, Iwate University, Morioka 020-8550, Japan. kiso@iwate-u.ac.jp
D015074:2-Aminoadipic Acid / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D000444:Aldehyde Dehydrogenase / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D001234:Aspergillus niger / Q000201:enzymology*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D012240:Rhodococcus / Q000201:enzymology*; D016415:Sequence Alignment
D001426:Bacterial Proteins; D005656:Fungal Proteins; C526190:N(alpha)-benzyloxycarbonyl-aminoadipic acid; D015074:2-Aminoadipic Acid; D000444:Aldehyde Dehydrogenase; D008239:Lysine