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Two malate dehydrogenases in Methanobacterium thermoautotrophicum
Archives of Microbiology, 1998Methanobacterium thermoautotrophicum (strain Marburg) was found to contain two malate dehydrogenases, which were partially purified and characterized. One was specific for NAD+ and catalyzed the dehydrogenation of malate at approximately one-third of the rate of oxalacetate reduction, and the other could equally well use NAD+ and NADP+ as coenzyme and ...
Thompson, H. +3 more
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1975
Publisher Summary The oxidation of L-malate in most living organisms is catalyzed by two distinct types of pyridine nucleotide-dependent enzymes. In one case the principal product is oxaloacetate, while in the other it is pyruvate and CO 2 .
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Publisher Summary The oxidation of L-malate in most living organisms is catalyzed by two distinct types of pyridine nucleotide-dependent enzymes. In one case the principal product is oxaloacetate, while in the other it is pyruvate and CO 2 .
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Solvent Interactions of Halophilic Malate Dehydrogenase
Biochemistry, 2002Malate dehydrogenase from the extreme halophilic Haloarcula marismortui (Hm MalDH) is an acidic protein that is unstable below molar salt concentrations. The solvated folded protein was studied by small-angle neutron scattering in solvents containing salt: NaCl, NaCH(3)CO(2), KF, NH(4)Cl, NH(4)CH(3)CO(2), (NH(4))(2)SO(4), MgCl(2), and MgSO(4).
Christine, Ebel +6 more
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Photosynthesis Research, 2006
NADP-dependent chloroplastic malate dehydrogenase (E.C.1.1.1.82) is regulated by thiol disulfide-interchange with thioredoxin. It displays two regulatory disulfides per subunit, located in specific sequence extensions respectively at the N- and C-terminal ends of each subunit.
Emmanuelle, Issakidis-Bourguet +4 more
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NADP-dependent chloroplastic malate dehydrogenase (E.C.1.1.1.82) is regulated by thiol disulfide-interchange with thioredoxin. It displays two regulatory disulfides per subunit, located in specific sequence extensions respectively at the N- and C-terminal ends of each subunit.
Emmanuelle, Issakidis-Bourguet +4 more
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Evolutionary relationships among the malate dehydrogenases
Trends in Biochemical Sciences, 1988Abstract The three-dimensional structures and elements essential for catalysis are conserved between mitochondrial and cytoplasmic forms of malate dehydrogenase in eukaryotic cells even though these isozymes are only marginally related at the level of primary structure.
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[19] Quantitation of malate, oxaloacetate, and malate dehydrogenase
1978Publisher Summary This chapter reviews the quantitation of l-malate and oxaloacetate using malate dehydrogenase and by monitoring the change in level of NADH with dehydrogenaseluciferase complex derived from Photobacterium fischeri. Malate dehydrogenase may be measured using the same approach, but with saturating levels of malate and excess NAD ...
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Asparate dehydrogenase activity of malate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964C R, SHAW, A L, KOEN
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Kepone inhibition of malate dehydrogenases
Journal of Agricultural and Food Chemistry, 1977B M, Anderson, C, Noble, E M, Gregory
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