Purification and Characterization of a Dehydrogenase Catalyzing Conversion of N^α-Benzyloxycarbonyl-L-Aminoadipic-δ-Semialdehyde to N^α-Benzyloxycarbonyl-L-Aminoadipic Acid from Rhodococcus sp. AIU Z-35-1(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNO
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概要
- 論文の詳細を見る
The enzyme catalyzing conversion of N^α-benzyloxycarbonyl-L-aminoadipic-δ-semialdehyde (N^α-Z-L-AASA) to N^α-benzyloxycarbonyl-L-aminoadipic acid (N^α-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 59kDa. The dehydrogenase exhibited enzyme activity on not only N^α-Z-L-AASA but also N^α-Z-D-AASA and short chain aliphatic aldehydes, but not on aromatic aldehydes and alcohols. The apparent K_m values for N^α-Z-L-AASA, N^α-Z-D-AASA and NAD^+ were estimated to be 3.8mM, 14.1mM and 0.16mM, respectively. The NH_2 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.
- 2007-11-25
著者
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Isobe Kimiyasu
The United Graduate School of Agricultural Sciences, Iwate University
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Isobe Kimiyasu
Department of Agro-bioscience, Faculty of Agriculture, Iwate University
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Fukuda Nahoko
Department of Agro-bioscience, Faculty of Agriculture, Iwate University
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Nagasawa Shouko
Department of Agro-bioscience, Faculty of Agriculture, Iwate University
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Isobe Kimiyasu
The United Graduate School Of Agricultural Sciences Iwate University
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Isobe Kimiyasu
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
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Fukuda Nahoko
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
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Nagasawa Shouko
Dep. Of Agro-bioscience Fac. Of Agriculture Iwate Univ.
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Nagasawa Shouko
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
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