Substrate Specificity and Stoichiometry of Nα-Benzyloxycarbonyl Amino Acid Urethane Hydrolase from Streptococcus faecalis R ATCC 8043
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概要
- 論文の詳細を見る
The substrate specificity of a new enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase, was investigated. The enzyme hydrolyzed Nα-benzyloxycarbonyl-glycine and -alanine, and Nα-benzoyl-glycine and -alanine. Nα-benzyloxycarbonyl-glycine was hydrolyzed to give equimolar benzyl alcohol and glycine. Equimolar benzoic acid and glycine were produced from Nα-benzoyl-glycine by the enzyme reaction. The Km, ko, and ko/Km values were measured for several substrates. The ko values varied widely with the amino acid residues. Nα-benzyloxycarbonyl-glycine and Nα-benzoyl-glycine produced relatively small changes in the Km values (0.36-0.10mM) and the ko/Km values (99440-2000M-1 sec-1). The rate of hydrolysis is significantly affected by electron-supplying substituents on the benzene ring.
- 社団法人 日本農芸化学会の論文
著者
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Murao Sawao
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Shin Takashi
Department Of Applied Microbial Technology Kumamoto Institute Of Technology
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Kawano Tatsu
Laboratory Of Microbial Products Osaka University Of Pharmaceutical Sciences
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MATSUMURA Eiko
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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SHIN Takashi
Department of Agricultural Chemistry, Faculty of Agriculture, University of Osaka Prefecture
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