Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1981 Dec 1;199(3):693–698. doi: 10.1042/bj1990693

A stereochemical investigation of phosphoryl transfer catalysed by phosphoglucomutase by the use of alpha-D-glucose 1-[(S)-16O,17O,18O]phosphate.

G Lowe, B V Potter
PMCID: PMC1163426  PMID: 6462135

Abstract

Rabbit muscle phosphoglucomutase converts alpha-D-glucose 1-[(S)-16O,17O,18O]phosphate into D-glucose 6-[16O,17O,18O]phosphate, which is shown by 31P n.m.r. spectroscopy, after cyclization and methylation, to have the (S)-configuration at the phosphorus atom. Since phosphoglucomutase is known to catalyse phosphoryl transfer by way of a phospho-enzyme intermediate, and since individual phosphoryl-transfer steps appear in general to occur with inversion of configuration, this observation is most simply interpreted in terms of a double-displacement mechanism with two phosphoryl-transfer steps.

Full text

PDF
697

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ATKINSON M. R., JOHNSON E., MORTON R. K. Equilibrium constants of phosphoryl transfer from C-1 to C-6 of alpha-D-glucose 1-phosphate and from glucose 6-phosphate to water. Biochem J. 1961 Apr;79:12–15. doi: 10.1042/bj0790012. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Blättler W. A., Knowles J. R. Phosphoglycerate mutases: stereochemical course of the phosphoryl group transfers catalyzed by the cofactor-dependent enzyme from rabbit muscle and the cofactor-independent enzyme from wheat germ. Biochemistry. 1980 Feb 19;19(4):738–743. doi: 10.1021/bi00545a020. [DOI] [PubMed] [Google Scholar]
  3. Britton H. G., Clarke J. B. The mechanism of the phosphoglucomutase reaction. Studies on rabbit muscle phosphoglucomutase with flux techniques. Biochem J. 1968 Nov;110(2):161–180. doi: 10.1042/bj1100161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Knowles J. R. Enzyme-catalyzed phosphoryl transfer reactions. Annu Rev Biochem. 1980;49:877–919. doi: 10.1146/annurev.bi.49.070180.004305. [DOI] [PubMed] [Google Scholar]
  5. Lowe G., Cullis P. M., Jarvest R. L., Potter B. V., Sproat B. S. Stereochemistry of phosphoryl transfer. Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26;293(1063):75–92. doi: 10.1098/rstb.1981.0062. [DOI] [PubMed] [Google Scholar]
  6. MILSTEIN C., SANGER F. An amino acid sequence in the active centre of phosphoglucomutase. Biochem J. 1961 Jun;79:456–469. doi: 10.1042/bj0790456. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ma C., Ray W. J., Jr Structural comparisons among the central complexes in the phosphoglucomutase system by means of spectral techniques. Biochemistry. 1980 Feb 19;19(4):751–759. doi: 10.1021/bi00545a022. [DOI] [PubMed] [Google Scholar]
  8. NAJJAR V. A., PULLMAN M. E. The occurrence of a group transfer involving enzyme (phosphoglucomutase) and substrate. Science. 1954 May 7;119(3097):631–634. doi: 10.1126/science.119.3097.631. [DOI] [PubMed] [Google Scholar]
  9. RAY W. J., Jr, ROSCELLI G. A. A KINETIC STUDY OF THE PHOSPHOGLUCOMUTASE PATHWAY. J Biol Chem. 1964 Apr;239:1228–1236. [PubMed] [Google Scholar]
  10. Ray W. J., Jr, Mildvan A. S. Arrangement of the phosphate-and metal-binding subsites of phosphoglucomutase. Intersubsite distance by means of nuclear magnetic resonance measurements. Biochemistry. 1973 Sep 11;12(19):3733–3743. doi: 10.1021/bi00743a024. [DOI] [PubMed] [Google Scholar]
  11. Ray W. J., Jr, Mildvan A. S., Long J. W. Arrangement of the phosphate-and metal-binding subsites of phosphoglucomutase. Intersubsite relationships by means of inhibition patterns. Biochemistry. 1973 Sep 11;12(19):3724–3732. doi: 10.1021/bi00743a023. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES