PMID: 6404748Jan 1, 1983Paper

Lipoamide dehydrogenase from baker's yeast. Improved purification and some molecular, kinetic, and immunochemical properties

Hoppe-Seyler's Zeitschrift für physiologische Chemie
P HeinrichG B Kresze

Abstract

The flavoprotein lipoamide dehydrogenase was purified, by an improved method, from commercial baker's yeast about 700-fold to apparent homogeneity with 50-80% yield. The enzyme had a specific activity of 730-900 U/mg (about twice the value of preparations described previously). The holoenzyme, but not the apoenzyme, possessed very high stability against proteolysis, heat, and urea treatment and could be reassociated, with fair yield, with the other components of yeast pyruvate dehydrogenase complex to give the active multienzyme complex. The apoenzyme was reactivated when incubated with FAD but not FMN. As other lipoamide dehydrogenases, the yeast enzyme was found to possess diaphorase activity catalysing the oxidation of NADH with various artificial electron acceptors. Km values were 0.48 mM for dihydrolipoamide and 0.15 mM for NAD. NADH was a competitive inhibitor with respect to NAD (Ki 31 microM). The native enzyme (Mr 117000) was composed of two apparently identical subunits (Mr 56000), each containing 0.96 FAD residues and one cystine bridge. The amino acid composition differed from bacterial and mammalian lipoamide dehydrogenases with respect to the content of Asx, Glx, Gly, Val, and Cys. The lipoamide dehydrogenases of ...Continue Reading

References

Oct 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·F H PettitL J Reed
Nov 22, 1965·Biochimica Et Biophysica Acta·A Wren, V Massey
Jan 1, 1968·Journal of Biochemistry·Y KawaharaK Nakanishi
May 1, 1959·Archives of Biochemistry and Biophysics·G L ELLMAN
Jan 1, 1952·The Journal of General Physiology·M KUNITZ

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