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Dehydrogenase nucleotide-dependent

The stereospecificity of hydrogen transfer for estradiol-17 and estradiol-17(3 dehydrogenases has been examined by George et a/.84>. These enzymes are both present in chicken liver, and have substrates which differ only in the chirality of their substituents at C—17. Both of these enzymes were shown to use the 4-pro-S or 4B proton of the NADPH. Since the steroid is a bulky substrate, the authors argue that the steric fit between pyridine nucleotide and steroid cannot be as important as the role played by the enzyme in directing the fit. This paper contains an interesting summary of other recent work on the stereospecificity of pyridine nucleotide dependent-steroid dehydrogenases. [Pg.56]

Pyridine nucleotide-dependent dehydrogenases (ed. H. Sund). Berlin—Heidelberg—New York Springer 1970. [Pg.67]

Pyridine nucleotide-dependent flavoenzyme catalyzed reactions are known for the external monooxygenase and the disulfide oxidoreductases However, no evidence for the direct participation of the flavin semiquinone as an intermediate in catalysis has been found in these systems. In contrast, flavin semiquinones are necessary intermediates in those pyridine nucleotide-dependent enzymes in which electron transfer from the flavin involves an obligate 1-electron acceptor such as a heme or an iron-sulfur center. Examples of such enzymes include NADPH-cytochrome P4S0 reductase, NADH-cytochrome bs reductase, ferredoxin — NADP reductase, adrenodoxin reductase as well as more complex enzymes such as the mitochondrial NADH dehydrogenase and xanthine dehydrogenase. [Pg.127]

Alcohol dehydrogenase is also obtained from yeast. Yeast alcohol dehydrogenase (YADH) was the first pyridine nucleotide-dependent dehydrogenase to be crystallized by Negelein and Wulff in 1937.1342 YADH is a tetramer of molecular weight 140000-150000. The amount of zinc determined varies,1343 but there are strong indications that the subunits of YADH and LADH have similar structures, including the presence of two zinc atoms. [Pg.1009]

C. I. Branddn, E. Zeppezauer, T. Boiwe, C. Sdderlund, B. O. Soderbeg and B. Nordstrom, in Pyridine Nucleotide Dependent Dehydrogenases , ed. H. Sund, Springer-Verlag, Berlin, 1970, p. 133. [Pg.1043]

Muscle tissue contains two glycerol-3-phosphate dehydrogenases a cytosolic enzyme, which uses NADH, and a flavin-nucleotide-dependent mitochondrial enzyme. What is the metabolic significance of these two enzymes ... [Pg.415]

Theorell, H. (1970) in H. Sund (Ed.), Pyridine Nucleotide-Dependent Dehydrogenases, Springer, Berlin, pp. 121-126. [Pg.156]

S. F. Velick tn Pyridine Nucleotide-Dependent Dehydrogenases (H. Sund, ed.), p. 57. Springer-Verlag, Berlin and New York, 1970. [Pg.9]

Jr., G. Zanetti, and S. Ronchi, in Pyridine Nucleotide-Dependent Dehydrogenases ... [Pg.146]

Eisele, B., Wallenfels, K. Pyridine nucleotide-dependent dehydrogenases (ed. H. Sund), p. 91. Berlin - Heidelberg - New York Springer 1970. [Pg.233]


See other pages where Dehydrogenase nucleotide-dependent is mentioned: [Pg.53]    [Pg.775]    [Pg.777]    [Pg.1016]    [Pg.240]    [Pg.5]    [Pg.269]    [Pg.255]    [Pg.158]    [Pg.33]    [Pg.147]    [Pg.775]    [Pg.777]    [Pg.44]    [Pg.1638]    [Pg.201]    [Pg.1081]    [Pg.33]   
See also in sourсe #XX -- [ Pg.777 ]

See also in sourсe #XX -- [ Pg.777 ]

See also in sourсe #XX -- [ Pg.777 ]

See also in sourсe #XX -- [ Pg.777 ]




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Dehydrogenases nucleotide

Pyridine nucleotide-dependent dehydrogenase

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