Phosphoglycerate mutase from Streptomyces coelicolor A3(2): purification and characterization of the enzyme and cloning and sequence analysis of the gene

PJ WHITE, J NAIRN, NC PRICE, HG NIMMO, J R Coggins, IS HUNTER

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12 Citations (Scopus)

Abstract

The enzyme 3-phosphoglycerate mutase was purified 192-fold from Streptomyces coelicolor, and its N-terminal sequence was determined. The enzyme is tetrameric with a subunit M(r) of 29,000. It is 2,3-bisphosphoglycerate dependent and inhibited hy vanadate. The gene encoding the enzyme was cloned by using a synthetic oligonucleotide probe designed from the N-terminal peptide sequence, and the complete coding sequence was determined. The deduced amino acid sequence is 64% identical to that of the phosphoglycerate mutase of Saccharomyces cerevisiae and has substantial identity to those of other phosphoglycerate mutases.

Original languageEnglish
Pages (from-to)434-440
Number of pages7
JournalJournal of Bacteriology
Volume174
Issue number2
Publication statusPublished - Jan 1992

Keywords

  • AMINO-ACID SEQUENCE
  • SCHIZOSACCHAROMYCES-POMBE
  • MOLECULAR-CLONING
  • CDNA

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