Acetate kinase: not just a bacterial enzyme

Trends Microbiol. 2006 Jun;14(6):249-53. doi: 10.1016/j.tim.2006.04.001. Epub 2006 May 4.


The bacterial enzymes acetate kinase (AK) and phosphotransacetylase (PTA) form a key pathway for synthesis of the central metabolic intermediate acetyl coenzyme A (acetyl-CoA) from acetate or for generation of ATP from excess acetyl-CoA. Putative AK genes have now been identified in some eukaryotic microbes. In Chlamydomonas reinhardtii and Phytophthora species, AK forms a pathway with PTA. AK has also been identified in non-yeast fungi but these fungi do not have PTA. Instead, AK forms a pathway with D-xylulose 5-phosphate phosphoketolase (XFP), a pathway that was also previously found only in bacteria. In Entamoeba histolytica, neither PTA nor XFP was found as a partner for AK. Thus, eukaryotic microbes seem to have incorporated the 'bacterial' enzyme AK into at least three different metabolic pathways.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Acetate Kinase / genetics*
  • Acetate Kinase / metabolism
  • Algal Proteins / genetics
  • Algal Proteins / metabolism
  • Amoeba / genetics
  • Amoeba / metabolism
  • Animals
  • Eukaryotic Cells / enzymology*
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Phosphate Acetyltransferase / genetics
  • Phosphate Acetyltransferase / metabolism
  • Phylogeny
  • Sequence Homology, Amino Acid*


  • Algal Proteins
  • Fungal Proteins
  • Phosphate Acetyltransferase
  • Acetate Kinase