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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Enzyme: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase

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

Summary:
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

Gene-Reaction Schematic: ?

MultiFun Terms: metabolism carbon utilization carbon compounds


Enzymatic reaction of: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase

EC Number: 5.4.2.12

2-phospho-D-glycerate <=> 3-phospho-D-glycerate

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)

Activators (Allosteric): Mg2+ [vanderOost02] , Mn2+ [vanderOost02] , Co2+ [vanderOost02]

Primary Physiological Regulators of Enzyme Activity: Mg2+

Kinetic Parameters:

Substrate
Km (μM)
Citations
3-phospho-D-glycerate
490.0
[vanderOost02]

T(opt): 100 °C [vanderOost02]

pH(opt): 8 [vanderOost02]


References

vanderOost02: van der Oost J, Huynen MA, Verhees CH (2002). "Molecular characterization of phosphoglycerate mutase in archaea." FEMS Microbiol Lett 212(1);111-20. PMID: 12076796


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, biocyc12.