The stereospecificity of the ferrous-ion-dependent alcohol dehydrogenase from Zymomonas mobilis
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چکیده
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Pyruvate decarboxylase from Zymomonas mobilis
To study the mechanism of re-activation of Zymomonas mobilis pyruvate decarboxylase apoenzyme by its cofactors thiamin diphosphate and Mg2", cofactor-free enzyme was prepared by dialysis against I mM-dipicolinic acid at pH 8.2. This apoenzyme was then used in a series of experiments that included determination of: (a) the affinity towards one cofactor when the other was present at saturating co...
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15 صفحه اولNucleotide sequence of the pyruvate decarboxylase gene from Zymomonas mobilis.
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CH4ts is a previously isolated recombinant mutant of Streptococcus mutans NG8 which produces a thermolabile L-(+)-lactate dehydrogenase (LDH) activity. It does not grow at 42 degrees C under a variety of cultivation conditions. In this study, we show that a batch culture of CH4ts shifted from 30 to 42 degrees C underwent rapid cessation of growth and accelerated cell death. The mutant grew at 4...
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Raps, Shirley (University of Illinois, Urbana) and R. D. DeMoss. Glycolytic enzymes in Zymomonas mobilis. J. Bacteriol. 84:115-118. 1962-An enzyme extract of Zymomonas mobilis (Pseudomonas lindneri) was capable of fermenting glucose-6-phosphate to CO(2) and ethanol. The extract was found to contain phosphohexoisomerase, aldolase, and glyceraldehyde-3-phosphate dehydrogenase, but no demonstrable...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1989
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1989.tb14658.x