Triphosphopyridine Nucleotide-linked Aldehyde Reductase

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TRIPHOSPHOPYRIDINE NUCLEOTIDE - CYTOCHROME c REDUCTASE IN LIVER

In yeast the reduction of ferricytochrome c by reduced triphosphopyridine nucleotide (TPNH2) is catalyzed by a flavoprotein, cytochrome c reductase, which contains flavin mononucleotide (FMN, riboflavin phosphate) as the prosthetic group (1). In animal tissue the reduction of ferricytochrome c by TPNHz has not yet been reported, although the reaction with reduced diphosphopyridine nucleotide (D...

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The conversion of isocitric acid to alpha-ketoglutarate has been demonstrated both in animal tissues (Martius, 1937; Krebs and Johnson, 1937; Adler et al., 1939; Ochoa, 1948) and in yeast (Kornberg and Pricer, 1951; Foulkes, 1951). Triphosphopyridine nucleotide was first implicated as a specific coenzyme for this reaction by Adler et al. (1939). Recently Kornberg and Pricer (1951) found in yeas...

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Diphosphopyridine Nucleotide - linked Aldehyde Dehydrogenase

In continuation of our investigation of liver diphosphopyridine nucleotide-linked aldehyde dehydrogenase (1)) we have undertaken a study of various classes of inhibitors of the enzyme. Interest in aldehyde oxidation has been increasing in recent years from several points of view. The classical problem of ethanol oxidation in viva still has many unresolved facets (Z), and the enzymes responsible...

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The biological role of reduced triphosphopyridine nucleotide (TPNH) and the metabolic pathways of its hydrogen atom and electron appear to be fundamentally different from those of reduced diphosphopyridine nucleotide (DPNH). The latter coenzyme appears to be intimately involved in cellular adenosine triphosphate (ATP) production, and is oxidized by both a phosphorylating, antimycin-sensitive pa...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1972

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)45010-2