The electron microscopic image of native cyclosporin synthetase molecules showed large globular complexes of 25 nm in diameter, built up by smaller interconnected units. Compartmentation of cyclosporin synthetase and the functionally interconnected D-alanine racemase was revealed after sucrose density gradient centrifugation of subcellular fractions and immunoelectron microscopy. A considerable proportion of cyclosporin synthetase and D-alanine racemase was detected at the vacuolar membrane. The product cyclosporin was localized in the fungal vacuole.
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Similar content being viewed by others Explore related subjectsDiscover the latest articles and news from researchers in related subjects, suggested using machine learning. Author information Authors and AffiliationsInstitut für Mikrobiologie und Genetik, Grisebachstrasse 8, 37077 Göttingen, Germany, , , , ,
Michael Hoppert & Carsten Gentzsch
Biochemie GmbH, 6250 Kundl, Austria, , , , ,
Kurt Schörgendorfer
Electronic Publication
About this article Cite this articleHoppert, M., Gentzsch, C. & Schörgendorfer, K. Structure and localization of cyclosporin synthetase, the key enzyme of cyclosporin biosynthesis in Tolypocladium inflatum. Arch Microbiol 176, 285–293 (2001). https://doi.org/10.1007/s002030100324
Received: 06 March 2001
Revised: 28 May 2001
Accepted: 08 June 2001
Issue Date: October 2001
DOI: https://doi.org/10.1007/s002030100324
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