Phosphoglycerate kinase

Phosphoglycerate kinase
Identifiers
EC no.2.7.2.3
CAS no.9001-83-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Phosphoglycerate kinase
Structure of yeast phosphoglycerate kinase.[1]
Identifiers
SymbolPGK
PfamPF00162
InterProIPR001576
PROSITEPDOC00102
SCOP23pgk / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Phosphoglycerate kinase (EC 2.7.2.3) (PGK 1) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP :

1,3-bisphosphoglycerate + ADP ⇌ glycerate 3-phosphate + ATP

Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-generating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, generating ADP and 1,3-BPG.

In humans, two isozymes of PGK have been so far identified, PGK1 and PGK2. The isozymes have 87-88% identical amino acid sequence identity and though they are structurally and functionally similar, they have different localizations: PGK2, encoded by an autosomal gene, is unique to meiotic and postmeiotic spermatogenic cells, while PGK1, encoded on the X-chromosome, is ubiquitously expressed in all cells.[2]

  1. ^ Watson HC, Walker NP, Shaw PJ, Bryant TN, Wendell PL, Fothergill LA, Perkins RE, Conroy SC, Dobson MJ, Tuite MF (1982). "Sequence and structure of yeast phosphoglycerate kinase". The EMBO Journal. 1 (12): 1635–40. doi:10.1002/j.1460-2075.1982.tb01366.x. PMC 553262. PMID 6765200.
  2. ^ Cite error: The named reference Chiarelli2012 was invoked but never defined (see the help page).

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