Due to maintenance work, this service will not be available Thursday August 21st between 7am and 8am CEST.
PROSITE documentation PDOC00330

Phosphoenolpyruvate carboxylase active sites


Phosphoenolpyruvate carboxylase (EC (PEPcase) catalyzes the irreversible β-carboxylation of phosphoenolpyruvate by bicarbonate to yield oxaloacetate and phosphate. The enzyme is found in all plants and in a variety of microorganisms. A histidine [1] and a lysine [2] have been implicated in the catalytic mechanism of this enzyme; the regions around these active site residues are highly conserved in PEPcase from various plants, bacteria and cyanobacteria and can be used as a signature patterns for this type of enzyme.

Last update:

December 2004 / Patterns and text revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

PEPCASE_1, PS00781; Phosphoenolpyruvate carboxylase active site 1  (PATTERN)

PEPCASE_2, PS00393; Phosphoenolpyruvate carboxylase active site 2  (PATTERN)


1AuthorsTerada K., Izui K.
TitleSite-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction.
SourceEur. J. Biochem. 202:797-803(1991).
PubMed ID1765093

2AuthorsJiao J.-A., Podesta F.E., Chollet R., O'Leary M.H., Andreo C.S.
TitleIsolation and sequence of an active-site peptide from maize leaf phosphoenolpyruvate carboxylase inactivated by pyridoxal 5'-phosphate.
SourceBiochim. Biophys. Acta 1041:291-295(1990).
PubMed ID2268676

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)