Escherichia coli d-Malate Dehydrogenase, a Generalist Enzyme Active in the Leucine Biosynthesis Pathway
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چکیده
منابع مشابه
Enzyme Biosynthesis in Escherichia Coli
Escherichia coli B synthesized beta-galactosidase and an enzyme system for D-xylose when exposed to lactose and xylose respectively in nitrogen-free media. The amount of beta-galactosidase formed in the absence of external nitrogen depended upon the nature of the medium in which the cells had originally been grown. Half as much of this enzyme was synthesized without exogenous nitrogen by cells ...
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The structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 A resolution. The crystals belonged to space group C2, with unit-cell parameters a = 146.0, b = 52.0, c = 168.9 A, beta = 102.2 degrees. The structure was determined with the molecular-replacement pipeline program BALBES and was refined to a final R factor of 18.6% (R(free) = 21.4%). The final model has ...
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Kinetic studies and chemical modification studies using diethylpyrocarbonate and iodoacetate were performed on malate dehydrogenase isolated from Escherichia coli. Product inhibition experiments indicate that this enzyme follows an ordered Bi Bi kinetic mechanism, similar to other dehydrogenases, while log V/K profiles reveal that one ionizing group with a pKa between 7.8 and 8.7 acts as a gene...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2014
ISSN: 0021-9258
DOI: 10.1074/jbc.m114.595363