Fructose 1,6-diphosphate and 3′,5′-cyclic AMP as positive effectors of pyruvate kinase in developing embryos

Mil'man, L S; Yurowitzki, Yu.G.

doi:10.1016/0005-2744(67)90101-5

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Phosphorylase B+4 Pi1

Inhibition Of Glyceraldehyde1

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1969

1980

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Cited by 24 publications

(2 citation statements)

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“…cAMP stimulated the oxidation of glutamate, a-ketoglutarate, and pyruvate by brain homogenates and mitochondria ; 5'-AMP had a similar effect (263 ). cAMP enhanced py ruvate kinase activity of loach embryos and overcame the inhibition of py ruvate kinase by A TP (264).…”

Section: Phosphorylase B+4 Pimentioning

confidence: 95%

Cyclic Amp

Jost¹,

Rickenberg²

1971

Annu. Rev. Biochem.

259

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Section: Phosphorylase B+4 Pimentioning

confidence: 95%

Cyclic Amp

Jost¹,

Rickenberg²

1971

Annu. Rev. Biochem.

259

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“…This postulated model is based on the following observations by previous workers. Embryonic pyruvate kinase is strongly activated by either FDP or 3',5'-cyclic AMP, and the activation is synergistic when both are present (Milman and Yurowitzki, 1967). Phosphofructokinases from liver fluke and from pig heart are inhibited by ATP but the inhibition is reversed by 3',5 '-cyclic AMP (Mansour and Mansour, 1962;Mansour, 1963).…”

Section: Inhibition Of Glyceraldehydementioning

confidence: 99%

Metabolic control and structure of glycolytic enzymes. VI. Competitive inhibition of yeast glyceraldehyde 3-phosphate dehydrogenase by cyclic adenosine monophosphate, adenosine triphosphate, and other adenine-containing compounds

Yang¹,

Deal²

1969

Biochemistry

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Developmental changes in the pyruvate kinase isozymes of coho salmon

Guderley¹,

Cardenas²

1979

J. Exp. Zool.

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Pyruvate kinase exists as two major isozymes in coho salmon. As in mammals and birds, one form is present in the early embryo and maintains a wide tissue distribution in adults. This salmonid type K shows anodal migration during electrophoresis at pH 7.5. The appearence of functional musculature in the developing embryos. In adult animals this second form is the only pyruvate kinase in muscle. Brain, kidney, liver and gill contain primarily the type K pyruvate kinase while heart contains both major forms along with three intermediate forms which presumably constitute a hybrid set. Since there is no additional isozyme restricted to gluconeogenic tissues, we conclude that a type L isozyme has not developed in these animals. The two major isozymes are immunologically distincy. Both forms are dubject to fructose 1,6-bisphosphate activation of phosphoenolpyruvate binding, but the magnitude of the effect is small. The affinities for phosphoenolpyruvate are similar, but salmon type K has hyperbolic saturation curves with this substrate and type M has sigmoidal saturation curves. While the immunological data indicates considerable divergence in structure, the kinetic parameters of the two forms have remained relatively similar.

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Fructose 1,6-diphosphate and 3′,5′-cyclic AMP as positive effectors of pyruvate kinase in developing embryos

Cited by 24 publications

References 7 publications

Cyclic Amp

Cyclic Amp

Metabolic control and structure of glycolytic enzymes. VI. Competitive inhibition of yeast glyceraldehyde 3-phosphate dehydrogenase by cyclic adenosine monophosphate, adenosine triphosphate, and other adenine-containing compounds

Developmental changes in the pyruvate kinase isozymes of coho salmon

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