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The phosphoglycerate mutases.

L A Fothergill-Gilmore1, H C Watson

  • 1Department of Biochemistry, University of Edinburgh, Scotland.

Advances in Enzymology and Related Areas of Molecular Biology
|January 1, 1989
PubMed
Summary
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Cofactor-dependent and independent phosphoglycerate mutases share similarities but differ in efficiency and evolutionary origin. Further research is needed to fully understand these enzyme families.

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Evolution

Background:

  • The phosphoglycerate mutase (PGM) family is well-studied, but some members require further investigation.
  • Cofactor-dependent monophosphoglycerate mutase (MPGM) and bisphosphoglycerate mutase (BPGM) are closely related, sharing similar sequences and catalyzing the same reactions.

Purpose of the Study:

  • To investigate the similarities and differences between cofactor-dependent MPGM and BPGM.
  • To explore the evolutionary relationship between cofactor-dependent and cofactor-independent MPGM.
  • To elucidate the reaction mechanisms and substrate specificities of these enzymes.

Main Methods:

  • Comparative analysis of amino acid sequences.
  • Kinetic studies to determine reaction rates and mechanisms.

Related Experiment Videos

  • Investigation of enzyme structure-function relationships.

    • Main Results:

    • Both MPGM and BPGM catalyze reactions via a ping-pong mechanism with a phosphohistidine intermediate.
    • MPGM is more efficient in interconverting 3- and 2-phosphoglycerates due to an additional phospho ligand at its active site.
    • BPGM is a more effective substrate for 1,3-bisphosphoglycerate, likely due to phospho-binding site arrangement.
    • Cofactor-independent MPGM represents a distinct evolutionary branch, with its relationship to cofactor-dependent forms requiring further clarification.

    Conclusions:

    • Cofactor-dependent MPGM and BPGM exhibit distinct kinetic properties and substrate preferences despite their close relationship.
    • The cofactor-independent MPGM may have arisen through gene duplication, but its precise evolutionary path relative to cofactor-dependent forms remains uncertain.
    • Further research is essential to fully characterize these enzymes and their evolutionary history.