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Title: sup 1 H and sup 51 V NMR studies of the interaction of vanadate and 2-vanadio-3-phosphoglycerate with phosphoglycerate mutase

Abstract

The formation of complexes of vanadate with 2-phosphoglycerate and 3-phosphoglycerate have been studied using {sup 51}V nuclear magnetic resonance spectroscopy. Signals attributed to two 2,3-diphosphoglycerate analogues, 2-vanadio-3-phosphoglycerate and 2-phospho-3-vanadioglycerate, were detected but were not fully resolved from signals of inorganic vanadate and the anhydride formed between vanadate and the phosphate ester moieties of the individual phosphoglycerates. Equilibrium constants for formation of the two 2,3-bisphosphate analogues were estimated as 2.5 M{sup {minus}1} for 2-vanadio-3-phosphoglycerate and 0.2 M{sup {minus}1} for 2-phospho-3-vanadioglycerate. The results of the binding study are fully consistent with noncooperativity in the binding of vanadiophosphoglycerate to the two active sites of phosphoglycerate mutase (PGM). The results obtained here are in accord with these vanadate-phosphoglycerate complexes being much more potent inhibitors of phosphoglycerate mutase than either monomeric or dimeric vanadate. These results strongly support the view that phosphoryl transfer in this enzyme involves a pentacoordinate phosphate intermediate and suggests that the two active sites operate independently of each other.

Authors:
; ;  [1]
  1. Simon Fraser Univ., Burnaby, British Columbia (Canada)
Publication Date:
OSTI Identifier:
5515305
Resource Type:
Journal Article
Journal Name:
Biochemistry; (United States)
Additional Journal Information:
Journal Volume: 31:10; Journal ID: ISSN 0006-2960
Country of Publication:
United States
Language:
English
Subject:
62 RADIOLOGY AND NUCLEAR MEDICINE; ISOMERASES; BIOCHEMICAL REACTION KINETICS; PHOSPHOLIPIDS; NUCLEAR MAGNETIC RESONANCE; NMR SPECTRA; PROTONS; VANADATES; VANADIUM 51; BARYONS; ELEMENTARY PARTICLES; ENZYMES; ESTERS; FERMIONS; HADRONS; INTERMEDIATE MASS NUCLEI; ISOTOPES; KINETICS; LIPIDS; MAGNETIC RESONANCE; NUCLEI; NUCLEONS; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; ORGANIC PHOSPHORUS COMPOUNDS; OXYGEN COMPOUNDS; PROTEINS; REACTION KINETICS; RESONANCE; SPECTRA; STABLE ISOTOPES; TRANSITION ELEMENT COMPOUNDS; VANADIUM COMPOUNDS; VANADIUM ISOTOPES; 550601* - Medicine- Unsealed Radionuclides in Diagnostics

Citation Formats

Liu, S, Gresser, M J, and Tracey, A S. sup 1 H and sup 51 V NMR studies of the interaction of vanadate and 2-vanadio-3-phosphoglycerate with phosphoglycerate mutase. United States: N. p., 1992. Web. doi:10.1021/bi00125a007.
Liu, S, Gresser, M J, & Tracey, A S. sup 1 H and sup 51 V NMR studies of the interaction of vanadate and 2-vanadio-3-phosphoglycerate with phosphoglycerate mutase. United States. doi:10.1021/bi00125a007.
Liu, S, Gresser, M J, and Tracey, A S. Tue . "sup 1 H and sup 51 V NMR studies of the interaction of vanadate and 2-vanadio-3-phosphoglycerate with phosphoglycerate mutase". United States. doi:10.1021/bi00125a007.
@article{osti_5515305,
title = {sup 1 H and sup 51 V NMR studies of the interaction of vanadate and 2-vanadio-3-phosphoglycerate with phosphoglycerate mutase},
author = {Liu, S and Gresser, M J and Tracey, A S},
abstractNote = {The formation of complexes of vanadate with 2-phosphoglycerate and 3-phosphoglycerate have been studied using {sup 51}V nuclear magnetic resonance spectroscopy. Signals attributed to two 2,3-diphosphoglycerate analogues, 2-vanadio-3-phosphoglycerate and 2-phospho-3-vanadioglycerate, were detected but were not fully resolved from signals of inorganic vanadate and the anhydride formed between vanadate and the phosphate ester moieties of the individual phosphoglycerates. Equilibrium constants for formation of the two 2,3-bisphosphate analogues were estimated as 2.5 M{sup {minus}1} for 2-vanadio-3-phosphoglycerate and 0.2 M{sup {minus}1} for 2-phospho-3-vanadioglycerate. The results of the binding study are fully consistent with noncooperativity in the binding of vanadiophosphoglycerate to the two active sites of phosphoglycerate mutase (PGM). The results obtained here are in accord with these vanadate-phosphoglycerate complexes being much more potent inhibitors of phosphoglycerate mutase than either monomeric or dimeric vanadate. These results strongly support the view that phosphoryl transfer in this enzyme involves a pentacoordinate phosphate intermediate and suggests that the two active sites operate independently of each other.},
doi = {10.1021/bi00125a007},
journal = {Biochemistry; (United States)},
issn = {0006-2960},
number = ,
volume = 31:10,
place = {United States},
year = {1992},
month = {3}
}