Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase
نویسندگان
چکیده
منابع مشابه
Malate dehydrogenase: distribution, function and properties.
Malate dehydrogenase (MDH) (EC 1.1.1.37) catalyzes the conversion of oxaloacetate and malate. This reaction is important in cellular metabolism, and it is coupled with easily detectable cofactor oxidation/reduction. It is a rather ubiquitous enzyme, for which several isoforms have been identified, differing in their subcellular localization and their specificity for the cofactor NAD or NADP. Th...
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In the course of preparing carbamyl phosphate synthetase from frog liver, a crystalline protein fraction was obtained which proved to be glutamate dehydrogenase. Because of the considerable interest in this enzyme and the striking differences in certain properties of this enzyme from different animal sources (l-6), it seemed of importance to study the kinetic properties of crystalline frog live...
متن کاملRegulation of Mitochondrial Malate Dehydrogenase
The effect of citrate on the structure and function of porcine heart mitochondrial malate dehydrogenase (EC 1.1.1.37) has been characterized. The native dimeric form of this enzyme is specifically activated by citrate in the NAD’ -+ NADH direction and inhibited by citrate in the NADH -+ NAD’ direction. It is proposed that citrate is bound at a regulatory site that is distinct from the catalytic...
متن کاملCrystallization of halophilic malate dehydrogenase from Halobacterium marismortui.
Malate dehydrogenase from the extreme halophile Halobacterium marismortui crystallizes in highly concentrated phosphate solution in space group 12 with cell dimensions a = 113.8 A, b = 122.8 A, c = 126.7 A, beta = 98.1 degrees. The halophilic enzyme was found to be unstable at lower concentrations of phosphate. It associates with unusually large amounts of water and salt, and the combined parti...
متن کاملKinetic studies of the regulation of mitochondrial malate dehydrogenase by citrate.
Mitochondrial malate dehydrogenase shows a complex regulation pattern in the presence of citrate. Previously published results indicate that this enzyme is activated by citrate in the NAD(+)----NADH direction and inhibited in the opposite direction. Moreover, high concentrations of L-malate or oxaloacetate produce deviations from the Michaelis-Menten behaviour. Results reported in this paper cl...
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ژورنال
عنوان ژورنال: Journal of Zhejiang University-SCIENCE B
سال: 2016
ISSN: 1673-1581,1862-1783
DOI: 10.1631/jzus.b1500219