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 language | English |
---|---|
Pages (from-to) | 190-194 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 517 |
Issue number | 1-3 |
DOIs | |
State | Published - Apr 24 2002 |
Externally published | Yes |
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