PMID: 37086May 15, 1979

Salts- induced oxidase activity of lipoamide dehydrogenase from pig heart

European Journal of Biochemistry
M Nakamura, I Yamazaki

Abstract

A weak NADH oxidase activity of lipoamide dehydrogenase at neutral pH is increased as much as 15-fold by the addition of KI or (NH4)2SO4. The addition of NAD+ shifts the optimum pH for the KI-induced oxidase activity from 6.3 to 5.5 without changing the maximum activity. The optimum pH is similarly shifted to 5.6 when sulfhyldryl groups of the enzyme are oxidized in the presence of small amount of cupric ion. The NADH: lipoamide and NADH: p-benzoquinone reductase activities are strongly inhibited by KI but both are increased by the presence of (NH4)2SO4. The known intermediate having a charge-transfer band at 530 nm can be seen upon an addition of NADH to the enzyme in the presence of (NH4)2SO4 but not in the presence of KI. The enzyme flavin is reductase by a stoichiometric amount of NADH when KI is present.

References

Apr 1, 1976·Archives of Biochemistry and Biophysics·K MaruyamaO Hayaishi
Mar 1, 1973·European Journal of Biochemistry·H v Muiswinkel-Voetberg, C VEEGER
Mar 2, 1971·Biochimica Et Biophysica Acta·M Dixon
Mar 1, 1974·The Biochemical Journal·J P Brown, R N Perham
May 25, 1970·FEBS Letters·P HemmerichC VEEGER
Sep 1, 1957·Archives of Biochemistry and Biophysics·B CHANCE
Mar 18, 1961·Biochimica Et Biophysica Acta·V MASSEY, C VEEGER
Jan 1, 1963·The Biochemical Journal·L W MAPSON, F A ISHERWOOD
Oct 8, 1962·Biochimica Et Biophysica Acta·C VEEGER, V MASSEY
Jan 15, 1960·Biochimica Et Biophysica Acta·V MASSEY

Citations

Feb 9, 1996·Biochemical Pharmacology·G P BiewengaA Bast

Related Concepts

Hydrogen-Ion Concentration
Valine Lipoamide Dehydrogenase
Myocardium
NADH
NADH, NADPH Oxidoreductases
Oxidation-Reduction
Salts
Spectrophotometry

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