Pyruvate Kinase

K. Uyeda

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Scopus citations


Pyruvate kinase catalyzes the last step of glycolysis which is important for generating adenosine triphosphate (ATP). Mammals express four major pyruvate kinase (PK) isozymes: muscle (M1), liver (L), erythrocyte (R), and the ubiquitous M2 types. All but the M1 isozyme exhibit positive cooperative kinetic behaviors upon binding the allosteric activator fructose-1,6-diphosphate and in the presence of increasing phosphoenolpyruvate (PEP) concentrations. All four isozymes are inhibited by phenylalanine. The l-PK isozyme activity is also inhibited by phosphorylation in response to glucagon. Consistent with its important role in regulating glucose metabolism and fat synthesis in liver, l-PK is also extensively regulated at the level of transcription. l-PK transcription increases in response to glucose and insulin and decreases in response to glucagon and high fat diets.

Original languageEnglish (US)
Title of host publicationEncyclopedia of Biological Chemistry
Subtitle of host publicationSecond Edition
PublisherElsevier Inc.
Number of pages3
ISBN (Electronic)9780123786319
ISBN (Print)9780123786302
StatePublished - Feb 15 2013


  • Allosteric enzyme
  • Cancer
  • Carbohydrate metabolism
  • Fat synthesis
  • Gluconeogenesis
  • Glycolysis
  • Lipogenesis
  • Pyruvate kinase
  • Regulation of glycolysis
  • Warburg effects

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology


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