Literature summary for 5.2.1.8 extracted from

Gourlay, L.J.; Angelucci, F.; Baiocco, P.; Boumis, G.; Brunori, M.; Bellelli, A.; Miele, A.E.
The three-dimensional structure of two redox states of cyclophilin A from Schistosoma mansoni. Evidence for redox regulation of peptidyl-prolyl cis-trans isomerase activity (2007), J. Biol. Chem., 282, 24851-24857.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme in reduced and oxidized state at 1.5 and 1.8 A resolution. Oxidized enzyme contains a disulfide bridge between C-terminal cysteines C122 and C126	Schistosoma mansoni

Inhibitors

Inhibitors	Comment	Organism	Structure
cyclosporin A	-	Schistosoma mansoni

Organism

Organism	UniProt	Comment	Textmining
Schistosoma mansoni	Q26548	cyclophilin A	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	mechanism for regulation of isoform cyclosporin A activity via oxidation of its thiol groups at C122 and C126, oxidized enzyme is inactive, whereas the reduced enzyme is an efficient isomerase	Schistosoma mansoni

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	ratio kcat/Km is 11000000 per M and s	Schistosoma mansoni

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide	-	Schistosoma mansoni	succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide	-	?

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.000014	-	10°C, pH 7.9	Schistosoma mansoni	cyclosporin A

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Release 2023.1 (January 2023)