PMID: 6411472Sep 15, 1983Paper

Affinity labelling of the allosteric site of the L-lactate dehydrogenase of Lactobacillus casei

European Journal of Biochemistry
R HenselC Woenckhaus

Abstract

Kinetic investigations employing the substrate analogues 2-oxoglutarate and phospho(enol)pyruvate indicate that the allosteric L-lactate dehydrogenase (EC 1.1.1.27) of Lactobacillus casei has a non-catalytic pyruvate-binding site to which, in addition to pyruvate, the allosteric effector fructose 1,6-bisphosphate can also be found. A modification using the 14C-labelled substrate analogue 3-bromopyruvate induces a loss of regulation by fructose 1,6-bisphosphate. The histidine residue labelled by 3-bromopyruvate is homologous to histidine-188 which is part of the anion-binding site of the non-allosteric vertebrate L-lactate dehydrogenases. Thus, the allosteric site of the allosteric L-lactate dehydrogenases corresponds to the anion-binding site of the non-allosteric vertebrate enzymes.

References

Jul 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·W EventoffH H Kiltz
Apr 25, 1976·Journal of Molecular Biology·J L WhiteM G Rossmann
Jan 1, 1971·Hoppe-Seyler's Zeitschrift für physiologische Chemie·J BerghäuserC Woenckhaus
Jun 5, 1973·Journal of Molecular Biology·M J AdamsM G Rossman
Sep 12, 1970·Nature·M J AdamsA J Wonacott

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Citations

Aug 11, 2011·Journal of Biochemistry·Kazuhito AraiHayao Taguchi
Feb 22, 1990·European Journal of Biochemistry·A WrbaK O Stetter
Dec 5, 1987·Journal of Molecular Biology·C Abad-ZapateroM G Rossmann
Sep 27, 2014·The Journal of Biological Chemistry·Yoko IkeharaHayao Taguchi
Sep 19, 2007·Molecular Cancer Therapeutics·Won KimHyo-Suk Lee
Aug 1, 1991·Applied and Environmental Microbiology·S F KimM Y Pack

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