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Literature summary for 5.2.1.8 extracted from

  • Galigniana, M.D.; Morishima, Y.; Gallay, P.A.; Pratt, W.B.
    Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex (2004), J. Biol. Chem., 279, 55754-55759.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
microtubule
-
Mus musculus 5874
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus general function of enzyme in binding of cargo for retrograde movement along microtubules ?
-
?
additional information Oryctolagus cuniculus general function of enzyme in binding of cargo for retrograde movement along microtubules ?
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Oryctolagus cuniculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information general function of enzyme in binding of cargo for retrograde movement along microtubules Mus musculus ?
-
?
additional information general function of enzyme in binding of cargo for retrograde movement along microtubules Oryctolagus cuniculus ?
-
?

Subunits

Subunits Comment Organism
More isoform Cyp-A exists in native heterocomplexes containing cytoplasmic dynein. Enzyme activity is not required for formation of dynein complexes. Binding to dynamitin is dependent on peptidylprolyl isomerase domain. Heterocomplexes containing tubulin and dynein can be formed in cytosol under microtubule-stabilizing conditions Oryctolagus cuniculus

Synonyms

Synonyms Comment Organism
cyclophilin-A
-
Oryctolagus cuniculus
cyp-A
-
Oryctolagus cuniculus