PMID: 7011400Jan 15, 1981Paper

Activation and inhibition of phosphoglycerate kinase by sulphate ion

Biochimica Et Biophysica Acta
M M Khamis, M Larsson-Raźnikiewicz

Abstract

A kinetic study of the effects of SO4(2-) in the activity of phosphoglycerate kinase (ATP: 3-phospho-D-glycerate 1-phosphotransferase, EC 2.7.2.3) is presented. SO4(2-) behaves both as an activator and inhibitor of the reaction. Activation does not appear to affect binding of one or the other of the two substrates to the catalytic centre. As an inhibitor SO4(2-) competes with both the substrates. Thus, each substrate can constrict SO4(2-) from the inhibitor binding site, probably the catalytic centre. Under these conditions activation becomes more and more evident. There appear to exist at least two SO4(2-) binding sites, one which earlier has been defined as an anion binding site, and a second, being the catalytic centre. The former seems to have a higher affinity for SO4(2-) than the latter.

References

Mar 16, 1976·European Journal of Biochemistry·P TanswellR J Williams
Apr 17, 1978·European Journal of Biochemistry·J A Wrobel, R A Stinson
Nov 2, 1978·European Journal of Biochemistry·R K Scopes
May 10, 1979·Biochimica Et Biophysica Acta·B Schierbeck, M Larsson-Raźnikiewicz
Mar 15, 1977·Biochimica Et Biophysica Acta·M L Raźnikiewicz, B Schierbeck
Jan 4, 1974·Nature·T N BryantP L Wendell
Nov 1, 1974·FEBS Letters·P TanswellR J Williams
Nov 7, 1972·European Journal of Biochemistry·M Larsson-Raźnikiewicz
Feb 1, 1973·FEBS Letters·M Larsson-Raźnikiewicz, J R. Jansson

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Citations

Mar 15, 1993·European Journal of Biochemistry·T PinedaJ E Churchich
Jul 1, 1992·European Journal of Biochemistry·P A WalkerH C Watson
May 31, 1990·European Journal of Biochemistry·W J FairbrotherR J Williams
Jul 15, 1989·European Journal of Biochemistry·P A WalkerH C Watson
Aug 15, 1993·European Journal of Biochemistry·H C João, R J Williams
Dec 1, 1994·Biophysical Chemistry·S J HendersonG J Bunick

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