Literature summary for 5.2.1.8 extracted from

Pirkl, F.; Buchner, J.
Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40 (2001), J. Mol. Biol., 308, 795-806.

Search for more literature for 5.2.1.8

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	the peptidylprolyl isomerase Cyp40, FKBP51 and FKBP52 are components of the Hsp90 chaperone complex. The peptidylprolyl isomerase monomers bind to a Hsp90 dimer. The three isomerase differ both in their affinity for Hsp90 and their chaperone activity suggesting that they play distinct roles in the Hsp90 chaperone complex	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the peptidylprolyl isomerase Cyp40, FKBP51 and FKBP52 are components of the Hsp90 chaperone complex. The peptidylprolyl isomerase monomers bind to a Hsp90 dimer. The three isomerase differ both in their affinity for Hsp90 and their chaperone activity suggesting that they play distinct roles in the Hsp90 chaperone complex	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	the peptidylprolyl isomerase Cyp40, FKBP51 and FKBP52 are components of the Hsp90 chaperone complex. The peptidylprolyl isomerase monomers bind to a Hsp90 dimer. The three isomerase differ both in their affinity for Hsp90 and their chaperone activity suggesting that they play distinct roles in the Hsp90 chaperone complex	Homo sapiens

Synonyms

Synonyms	Comment	Organism
Cyp40	-	Homo sapiens
FKBP51	-	Homo sapiens
FKBP52	-	Homo sapiens

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Release 2023.1 (January 2023)