Active subunits in hybrid-modified malate dehydrogenase.
نویسندگان
چکیده
منابع مشابه
Automatic classification of highly related Malate Dehydrogenase and L-Lactate Dehydrogenase based on 3D-pattern of active sites
Accurate protein function prediction is an important subject in bioinformatics, especially wheresequentially and structurally similar proteins have different functions. Malate dehydrogenaseand L-lactate dehydrogenase are two evolutionary related enzymes, which exist in a widevariety of organisms. These enzymes are sequentially and structurally similar and sharecommon active site residues, spati...
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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...
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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 کاملautomatic classification of highly related malate dehydrogenase and l-lactate dehydrogenase based on 3d-pattern of active sites
accurate protein function prediction is an important subject in bioinformatics, especially wheresequentially and structurally similar proteins have different functions. malate dehydrogenaseand l-lactate dehydrogenase are two evolutionary related enzymes, which exist in a widevariety of organisms. these enzymes are sequentially and structurally similar and sharecommon active site residues, spati...
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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: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)68401-2