On the Mechanism of Dihydrothioctyl Dehydrogenase Reaction
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چکیده
منابع مشابه
Kinetic studies on the mechanism of the malate dehydrogenase reaction.
This work is a kinetic investigation of the reaction mechanism of malate dehydrogenase, prepared from washed mince of whole bovine heart by a variation on previous methods. The forward and reverse reactions catalyzed by this enzyme have been studied at pH 8.0 in the presence and in the absence of one product at a time, with the use of a recording fluorometer to measure changes in the concentrat...
متن کاملStudies on the mechanism of the malate dehydrogenase reaction.
The stereospecificity of the chicken heart mitochondrial malate dehydrogenase as well as the ability of this enzyme to form various abortive complexes has been further investigated. The enzyme was found to be specific for the A-hydrogen of NADH. Complex formation of the enzyme with oxalacetate and oxidized coenzymes is pH-dependent and is promoted at alkaline pH values. The enol form of oxalace...
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cells remaining in a sonically disintegrated preparation fix with twice the efficiency of comparable whole cell controls. The crucial question, of course, is not the magnitude of the observed fixation, but is it real or only an experimental artifact arising from the whole cells remaining in the preparation. Routine counting established that intact cells ranged between 104-105/ml. Controls using...
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قاعده مقتضی و مانع در متون فقهی کم و بیش مستند احکام قرار گرفته و مورد مناقشه فقهاء و اصولیین می باشد و مشهور معتقند مقتضی و مانع، قاعده نیست بلکه یکی از مسائل ذیل استصحاب است لذا نگارنده بر آن شد تا پیرامون این قاعده پژوهش جامعی انجام دهد. به عقیده ما مقتضی دارای حیثیت مستقلی است و هر گاه می گوییم مقتضی احراز شد یعنی با ماهیت مستقل خودش محرز گشته و قطعا اقتضاء خود را خواهد داشت مانند نکاح که ...
15 صفحه اولMechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase.
Allylamine did not serve as an efficient substrate for methylamine dehydrogenase (EC 1.4.99.3) in a steady-state assay of activity and appeared to act as a competitive inhibitor of methylamine oxidation by methylamine dehydrogenase. Transient kinetic studies, however, revealed that allylamine rapidly reduced the tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrogenase. The rate ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1960
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)64651-4