A divergent archaeal member of the alkaline phosphatase binuclear metalloenzyme superfamily has phosphoglycerate mutase activity

David E. Graham, Huimin Xu, Robert H. White

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

The hyperthermophilic archaeon Methanococcus jannaschii uses several non-canonical enzymes to catalyze conserved reactions in glycolysis and gluconeogenesis. A highly diverged gene from that organism has been proposed to function as a phosphoglycerate mutase. Like the canonical cofactor-independent phosphoglycerate mutase and other members of the binuclear metalloenzyme superfamily, this M. jannaschii protein has conserved nucleophilic serine and metal-binding residues. Yet the substrate-binding residues are not conserved. We show that the genes at M. jannaschii loci MJ0010 and MJ1612 encode thermostable enzymes with phosphoglycerate mutase activity. Phylogenetic analyses suggest that this gene family arose before the divergence of the archaeal lineage.

Original languageEnglish
Pages (from-to)190-194
Number of pages5
JournalFEBS Letters
Volume517
Issue number1-3
DOIs
StatePublished - Apr 24 2002
Externally publishedYes

Funding

We thank Tom Glass for assistance with NMR analysis. This work was supported by U.S. National Science Foundation Grant MCB 9985712 to R.H.W.

Keywords

  • Alkaline phosphatase superfamily
  • Archaea
  • Gluconeogenesis
  • Glycolysis
  • Phosphoglycerate mutase

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