We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00330Phosphoenolpyruvate carboxylase active sites
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00330
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
PROSITE methods (with tools and information) covered by this documentation:
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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