Purification and characterization of a dehydrogenase catalyzing conversion of N alpha-benzyloxycarbonyl-L-aminoadipic-delta-semialdehyde to N alpha-benzyloxycarbonyl-L-aminoadipic acid from rhodococcus sp. AIU Z-35-1.
The enzyme catalyzing conversion of N alpha-benzyloxycarbonyl-L-aminoadipic-delta-semialdehyde (N alpha-Z-L-AASA) to N alpha-benzyloxycarbonyl-L-aminoadipic acid (N alpha-Z-L-AAA) in Rhodococcus sp. AIU Z-35-1 was identified, and its characteristics were revealed. This reaction was catalyzed by a dehydrogenase with a molecular mass of 59 kDa. The dehydrogenase exhibited enzyme activity on not only N alpha-Z-L-AASA but also N alpha-Z-D-AASA and short chain aliphatic aldehydes, but not on aromatic aldehydes and alcohols. The apparent Km values for N alpha-Z-L-AASA, N alpha-Z-D-AASA and NAD+ were estimated to be 3.8 mM, 14.1 mM and 0.16 mM, respectively. The NH2 terminal amino acid sequence of this enzyme exhibited a similarity to those of a piperidein-6-carboxylate dehydrogenase from Streptomyces clavuligerus and a putative dehydrogenase from Rhodococcus sp. RHA 1, but not to those of other microbial aldehyde dehydrogenases.
Isobe
Kimiyasu
K
Department of Agro-bioscience, Faculty of Agriculture, Iwate University, 3 Ueda, Morioka 020-8550, Japan. kiso@iwate-u.ac.jp <kiso@iwate-u.ac.jp>
Fukuda
Nahoko
N
Nagasawa
Shouko
S
D015074:2-Aminoadipic Acid / Q000031:analogs & derivatives* / Q000096:biosynthesis / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D002384:Catalysis; D008969:Molecular Sequence Data; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D012240:Rhodococcus / Q000201:enzymology*; D013379:Substrate Specificity
D001426:Bacterial Proteins; C526190:N(alpha)-benzyloxycarbonyl-aminoadipic acid; C505609:N(alpha)-benzyloxycarbonylaminoadipic acid delta-semialdehyde; D015074:2-Aminoadipic Acid; D000587:Oxidoreductases Acting on CH-NH Group Donors; C109029:delta-1-piperideine-6-carboxylate dehydrogenase