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Literature summary for 5.2.1.8 extracted from

  • Zydowsky, L.D.; Etzkorn, F.A.; Chang, H.Y.; Ferguson, S.B.; Stolz, L.A.; Ho, S.I.; Walsh, C.T.
    Active site mutants of human cyclophilin A separate peptidyl-prolyl isomerase activity from cyclosporin A binding and calcineurin inhibition (1992), Protein Sci., 1, 1092-1099.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q, expressed in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
F133A mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not Homo sapiens
F60A mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not Homo sapiens
H126Q mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not Homo sapiens
H47Q mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not Homo sapiens
Q111A mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not Homo sapiens
R55A mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not Homo sapiens
W121A mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 wild-type and mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glyceraldehyde 3-phosphate
-
 Homo sapiens Glycerone phosphate
-
 ?