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Literature summary for 5.2.1.8 extracted from

  • Golbik, R.; Fischer, G.; Fersht, A.R.
    Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18) (1999), Protein Sci., 8, 1505-1514.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
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Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
barstar C40A/C82A/P27A the mutant of barstar lacks complications arising from oxidation of Cys in wild-type or isomerization affecting the peptidyl-Pro27 bond. Refolding is comprised by several kinetically detectable folding phases. The slowest phase in refolding, the trans to cis isomerization of the Tyr47-Pro48 peptide bond being in cis conformation in the native state Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
Cyclophilin
-
Homo sapiens
Cyp18
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Homo sapiens