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Characterization of the Gene Cluster CYP264B1‐ geo A from Sorangium cellulosum So ce56: Biosynthesis of (+)‐Eremophilene and Its Hydroxylation
Author(s) -
Schifrin Alexander,
Ly Thuy T. B.,
Günnewich Nils,
Zapp Josef,
Thiel Verena,
Schulz Stefan,
Hannemann Frank,
Khatri Yogan,
Bernhardt Rita
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402443
Subject(s) - gene cluster , biosynthesis , farnesyl pyrophosphate , hydroxylation , biochemistry , escherichia coli , stereochemistry , gene , chemistry , farnesyl diphosphate synthase , mevalonate pathway , terpenoid , biology , enzyme
Terpenoids can be found in almost all forms of life; however, the biosynthesis of bacterial terpenoids has not been intensively studied. This study reports the identification and functional characterization of the gene cluster CYP264B1– geo A from Sorangium cellulosum So ce56. Expression of the enzymes and synthesis of their products for NMR analysis and X‐ray diffraction were carried out by employing an Escherichia coli whole‐cell conversion system that provides the geoA substrate farnesyl pyrophosphate through simultaneous overexpression of the mevalonate pathway genes. The geoA product was identified as a novel sesquiterpene, and assigned NMR signals unambiguously proved that geoA is an (+)‐eremophilene synthase. The very tight binding of (+)‐eremophilene (∼0.40 μ M ), which is also available in S. cellulosum So ce56, and its oxidation by CYP264B1 suggest that the CYP264B1– geo A gene cluster is required for the biosynthesis of (+)‐eremophilene derivatives.