A seventeen kilodaltons peptidyl-prolyl cis-trans isomerase of the cyclosporin-producer Tolypocladium inflatum is sensitive to cyclosporin A.
A peptidyl-prolyl cis-trans isomerase (PPIase) was purified to homogeneity about 24-fold from the cyclosporin-producing fungus Tolypocladium inflatum. The molecular mass of the enzyme was in the range of 17 kdaltons. Remarkably, the enzyme could be inhibited by cyclosporin A in the nanomolar range as has been shown for numerous other cyclophilins from eukaryotic organisms. This indicates, that Tolypocladium inflatum must possess a self protection system in order to survive in the presence of cyclosporin.
Zocher
R
R
Institut für Biochemie der Technischen, Universität Berlin, Germany.
Keller
U
U
Lee
C
C
Hoffmann
K
K
D000591:Amino Acid Isomerases / Q000737:chemistry / Q000302:isolation & purification*; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification*; D016572:Cyclosporine / Q000378:metabolism*; D003904:Mitosporic Fungi / Q000201:enzymology*; D008970:Molecular Weight; D019696:Peptidylprolyl Isomerase
D002352:Carrier Proteins; D016572:Cyclosporine; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase