A Study of the Mechanism of the Reactions Catalyzed by the Amidase Brevibacterium sp. R312(Biological Chemistry)
スポンサーリンク
概要
- 論文の詳細を見る
Besides its amide hydrolase activity, the amidase from Brevibacterium sp. R312 also exhibits an acyl-transferase activity. The mechanism of the transfer reaction of the acyl from acetamide to hydroxylamine was studied. This is a "Bi Bi Ping Pong" type reaction. The kinetic parameters of the reaction were determined: -Apparent V_m=135 μmol・min^<-1>・mg^<-1> -Acetamide K_m=18.2mM -Hydroxylamine K_m= 131 mM A reaction mechanism involving the -SH group of the amidase was proposed.
- 社団法人日本農芸化学会の論文
- 1986-09-23
著者
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Thiery Alain
Chaire De Genetique Et Microbiologie Ecole Nationale Superieure Agronomique
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MAESTRACCI Marc
Chaire de Genetique et Microbiologie, Ecole Nationale Superieure Agronomique
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ARNAUD Alain
Chaire de Genetique et Microbiologie, Ecole Nationale Superieure Agronomique
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GALZY Pierre
Chaire de Genetique et Microbiologie, Ecole Nationale Superieure Agronomique
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Galzy Pierre
Chaire De Genetique Et Microbiologie Ecole Nationale Superieure Agronomique
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Arnaud Alain
Chaire De Genetique Et Microbiologie Ecole Nationale Superieure Agronomique
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Maestracci Marc
Chaire De Genetique Et Microbiologie Ecole Nationale Superieure Agronomique
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GALZY PIERRE
Chaire de Genetique et Microbiologie , ENSA-INRA
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GALZY Pierre
Chaire de Génétique et Microbiologie, INRA-ENSA
関連論文
- A Study of the Mechanism of the Reactions Catalyzed by the Amidase Brevibacterium sp. R312(Biological Chemistry)
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