PROSITE documentation PDOC00330Phosphoenolpyruvate carboxylase active sites
Description
Phosphoenolpyruvate carboxylase (EC 4.1.1.31) (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.
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Technical section
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References
| 1 | Authors | Terada K. Izui K. |
| Title | Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction. | |
| Source | Eur. J. Biochem. 202:797-803(1991). | |
| PubMed ID | 1765093 |
| 2 | Authors | Jiao J.-A. Podesta F.E. Chollet R. O'Leary M.H. Andreo C.S. |
| Title | Isolation and sequence of an active-site peptide from maize leaf phosphoenolpyruvate carboxylase inactivated by pyridoxal 5'-phosphate. | |
| Source | Biochim. Biophys. Acta 1041:291-295(1990). | |
| PubMed ID | 2268676 |
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