Pyruvate kinase

Pyruvate kinase
3D structure of pyruvate kinase (1PKN)
Identifiers
EC no.2.7.1.40
CAS no.9001-59-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
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NCBIproteins

Pyruvate kinase is the enzyme involved in the last step of glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), yielding one molecule of pyruvate and one molecule of ATP.[1] Pyruvate kinase was inappropriately named (inconsistently with a conventional kinase) before it was recognized that it did not directly catalyze phosphorylation of pyruvate, which does not occur under physiological conditions.[2] Pyruvate kinase is present in four distinct, tissue-specific isozymes in animals, each consisting of particular kinetic properties necessary to accommodate the variations in metabolic requirements of diverse tissues.

  1. ^ Gupta V, Bamezai RN (November 2010). "Human pyruvate kinase M2: a multifunctional protein". Protein Science. 19 (11): 2031–44. doi:10.1002/pro.505. PMC 3005776. PMID 20857498.
  2. ^ Goodman HM (2009). Basic Medical Endocrinology (4th ed.). Elsevier. p. 132. ISBN 978-0-12-373975-9.