Substrate specificity of bovine liver formaldehyde dehydrogenase.
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چکیده
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Dual nucleotide specificity of bovine glutamate dehydrogenase
The thionicotinamide analogues of NAD+ and NADP+ were shown to be good alternative coenzymes for bovine glutamate dehydrogenase, with similar affinity and approx. 40% of the maximum velocity obtained with the natural coenzymes. Both thionicotinamide analogues show non-linear Lineweaver-Burk plots, which with the natural coenzymes have been attributed to negative co-operativity. Since the reduce...
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A comparison of rat and human liver formaldehyde dehydrogenase.
An NADand GSH-dependent formaldehyde dehydrogenase (formaldehyde: NAD* oxidoreductase, EC 1.2.I.Z) was purified from rat and human liver, and the properties of these enzymes were compared. The GSH requirement of the enzyme obtained from both species could not be replaced by dithiothreitol, CoA or cysteine, and NADP could not substitute for NAD. The pH optimum, and the Km of formaldehyde and NAD...
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The results obtained led the authors to the suggestion that Reactions 2 and 4 are catalyzed by liver alcohol dehydrogenase but that Reaction 1 is due to an aldehyde dehydrogenase present in their liver preparation. Because of the inhomogeneity of the enzyme preparation employed, a reinvestigation of this problem with more highly purified enzyme was suggested. With the use of crystalline horse l...
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The investigation of the substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli allows a description of the binding region of pyruvate. Substrate analogs with electronegative substitutions in the methyl group show a strong competitive inhibition of the overall reaction of the pyruvate dehydrogenase complex. The most efficient inhibitor is fluoropyruvate which has a mo...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1986
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)67010-3