|Gene:||pgm||Accession Number: G-3786 (MetaCyc)|
Synonyms: PF1959, iPGM
Species: Pyrococcus furiosus
Subunit composition of
2,3-bisphosphoglycerate-independent phosphoglycerate mutase = [Pgm]4
phosphoglycerate mutase subunit = Pgm
The interconversion of 3-phosphoglycerate and 2-phosphoglycerate during glycolysis and gluconeogenesis is catalyzed by phosphoglycerate mutase (PGM). In bacteria and eukaryotes two structurally distinct enzymes have been found, a cofactor-dependent (dPGM) and a cofactor-independent (iPGM) type.
Archaebacteria possess a new family of PGM proteins, distantly related to iPGMs. The P. furiosus enzyme has been cloned and expressed in a heterlogous host, and the activity of a cofactor-independent phosphoglycerate mutase has been confirmed [vanderOost02].
|Map Position: [1,808,901 -> 1,810,136]|
Molecular Weight of Polypeptide: 45.3 kD (experimental) [vanderOost02 ]
Molecular Weight of Multimer: 183.5 kD (experimental) [vanderOost02]
Unification Links: Entrez-gene:1469841
|MultiFun Terms:||metabolism → carbon utilization → carbon compounds|
Enzymatic reaction of: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
This reaction is reversible.
In Pathways: glycolysis V (Pyrococcus)
Primary Physiological Regulators of Enzyme Activity: Mg2+
T(opt): 100 °C [vanderOost02]
pH(opt): 8 [vanderOost02]
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