Dehalogenation and Deamination of L-2-Amino-4-chloro-4-pentenoic Acid by Proteus mirabilis(Biological Chemistry)
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概要
- 論文の詳細を見る
Eighty-one strains of bacteria were tested for their ability to catalyze the release of chloride ion from DL-2-amino-4-chloro-4-pentenoic acid. A dehalogenating enzyme was obtained from the cells of Proteus mirabilis IFO 3849, which can use the L-isomer. The enzyme was constitutively produced. The conversion of L-2-amino-4-chloro-4-pentenoic acid to 2-keto-4-pentenoic acid, ammonia, and chloride ion was demonstrated. The reaction product, 2-keto-4-pentenoic acid, was isolated as its 2,4-dinitrophenylhydrazone and identified by catalytic hydrogenolysis of the hydrazone to the corresponding amino acid, norvaline.
- 社団法人日本農芸化学会の論文
- 1987-12-23
著者
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Hatanaka Shin-ichi
Department Of Applied Physics And Chemistry The University Of Electro-communications
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Hatanaka Shin-ichi
Department Of Biology College Of Arts And Sciences The University Of Tokyo
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Moriguchi Mitsuaki
Department Of Environmental Chemistry And Engineering Faculty Of Engineering Oita University
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Moriguchi Mitsuaki
Department Of Applied Chemistry Faculty Of Engineering Oita University
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HOSHINO Seiichi
Department of Environmental Chemistry and Engineering, Faculty of Engineering, Oita University
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Hoshino Seiichi
Department Of Environmental Chemistry And Engineering Faculty Of Engineering Oita University
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