منابع مشابه
Regulation 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 کاملTHE EFFECT OF SALT STRESS ON MALATE DEHYDROGENASE IN WHEAT
Effect of various NaCI treatments (0, 50, 100, 200 and 300 mM) at different growth and development stages (tillering, boot swollen, flowering and anthesis) of two wheat cultivars on the kinetic activity and PAGE electrophoretic pattern of leaf malate dehydrogenase was studied under greenhouse conditions. Ghods was salt-sensitive and Boolani was salt-tolerant. In general, in response to salinti...
متن کاملConvergent evolution of Trichomonas vaginalis lactate dehydrogenase from malate dehydrogenase.
Lactate dehydrogenase (LDH) is present in the amitochondriate parasitic protist Trichomonas vaginalis and some but not all other trichomonad species. The derived amino acid sequence of T. vaginalis LDH (TvLDH) was found to be more closely related to the cytosolic malate dehydrogenase (MDH) of the same species than to any other LDH. A key difference between the two T. vaginalis sequences was tha...
متن کاملMalate 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...
متن کاملSubunit Interactions in Mitochondrial Malate Dehydrogenase
The pH-dependent dissociation of porcine heart mitochondrial malate dehydrogenase (t-malate:NAD+ oxidoreductase, EC 1.1.1.37) has been more extensively characterized. "he native, dimeric form of the enzyme (Mr = 70,000) which exists at pH 7.5 has previously been shown to dissociate into its constituent subunits (Mr = 35,000) at pH 5.0 (Bleile, D. M., Schulz, R. A., Gregory, E. M., and Harrison,...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43471-6