Purification and Properties of an Alcohol Dehydrogenase (ADHc) of a Mutant Strain of Schwanniomyces castellii : SC-ADH-5P
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概要
- 論文の詳細を見る
Alcohol dehydrogenase (alcohol NAD^+ oxidoreductase, EC 1.1.1.1) from Schwanniomyces castellii SCADH 5P strain has been purified 54-fold by affinity chromatography on Cibacron-blue. The enzyme is monomeric and has a molecular weight of 45000. The kinetic studies show that the mechanism of reaction is only compatible with an ordered sequential mechanism in which the cofactor is the first fixed substrate. The enzyme was found to oxidize primary alcohols and pliphatic aldehydes. The presence of an "α" double bond increases the enzyme activity both for alcohols and aldehydes.
- 社団法人日本生物工学会の論文
- 1989-12-25
著者
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GALZY Pierre
Chaire de Genetique et Microbiologie, Ecole Nationale Superieure Agronomique
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Moulin G
Ensa Montpellier Fra
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Moulin Guy
Chaire De Genetique Et Microbiologie Ensa-inra
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MOUILLET-LOEVENBRUCK DOROTHEE
Chaire de Genetique et Microbiologie , ENSA-INRA
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NICOLAS MICHEL
Laboratoire de Biologie Cellulaire et Moleculaire, INSERM U65, USTL, place E. Bataillon
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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 Ensa-inra
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Mouillet-loevenbruck Dorothee
Chaire De Genetique Et Microbiologie Ensa-inra
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Nicolas Michel
Laboratoire De Biologie Cellulaire Et Moleculaire Inserm U65 Ustl Place E. Bataillon
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GALZY PIERRE
Chaire de Genetique et Microbiologie , ENSA-INRA
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MOULIN GUY
Chaire de Genetique et Microbiologie , ENSA-INRA
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GALZY Pierre
Chaire de Génétique et Microbiologie, INRA-ENSA
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