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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

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