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PROSITE documentation PDOC00840 [for PROSITE entry PS50198] |
Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) (PPIase or rotamase) is an enzyme that accelerates protein folding by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides [1]. Most characterized PPiases belong to two families, the cyclophilin-type (see <PDOC00154>) and the the FKBP-type (see <PDOC00426>). Recently a third family has been discovered [2,3]. So far, the only biochemically characterized member of this family is the Escherichia coli protein parvulin (gene ppiC), a small (92 residues) cytoplasmic enzyme that prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates. PpiC is evolutionary related to a number of proteins that are also probably PPiases:
As a signature pattern, we selected a conserved region that contains a serine which could play a role in the catalytic mechanism of these enzymes. We also developed a profile that spans the complete ppiC domain.
Expert(s) to contact by email: Last update:December 2001 / Text revised; profile added.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Fischer G. Schmid F.X. |
Title | The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell. | |
Source | Biochemistry 29:2205-2212(1990). | |
PubMed ID | 2186809 |
2 | Authors | Rudd K.E. Sofia H.J. Koonin E.V. Plunkett G. III Lazar S. Rouviere P.E. |
Source | Trends Biochem. Sci. 20:14-15(1995). |
3 | Authors | Rahfeld J.-U. Rucknagel K.P. Schelbert B. Ludwig B. Hacker J. Mann K. Fischer G. |
Title | Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin. | |
Source | FEBS Lett. 352:180-184(1994). | |
PubMed ID | 7925971 |