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.

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. Research Abstract Details 

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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. Abstract Text:

Kimiyasu Isobe,Nahoko Fukuda,Shouko Nagasawa,Kimiyasu Isobe,Nahoko Fukuda,Shouko Nagasawa,Kimiyasu Isobe,Nahoko Fukuda,Shouko Nagasawa,

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 K(m) 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 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.

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. Publishing Authors By Initials

K Isobe,N Fukuda,S Nagasawa,K Isobe,N Fukuda,S Nagasawa,K Isobe,N Fukuda,S Nagasawa,

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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. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of bioscience and bioengineering

VOLUME: 104

Page Numbers: 398-402

Journal Abbreviation: J. Biosci. Bioeng.

ISSN: 1389-1723

DAY: 18

MONTH: Nov

YEAR: 2007

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. Information

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LANGUAGE: eng

NlmUniqueID: 100888800

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. Keywords Mesh Terms:

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AFFILIATION: Department of Agro-bioscience, Faculty of Agriculture, Iwate University, 3 Ueda, Morioka 020-8550, Japan.

Country: Japan

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Purification and Characterization of a Dehydrogenase Catalyzing Conversion of Nalpha-Benzyloxycarbonyl-L-Aminoadipic-delta-Semialdehyde to Nalpha-Benzyloxycarbonyl-L-Aminoadipic Acid from Rhodococcus sp AIU Z-35-1 Related Publications

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