RRC ID 17459
Author Sato T, Takizawa K, Orito Y, Kudo H, Hoshino T.
Title Insight into C35 terpene biosyntheses by nonpathogenic Mycobacterium Species: functional analyses of three Z-prenyltransferases and identification of dehydroheptaprenylcyclines.
Journal Chembiochem
Abstract Nonpathogenic Mycobacterium species produce rare cyclic C(35) terpenes that are biosynthesized by cyclization of Z-type C(35) polyprenyl diphosphate. To provide deeper insight into the biosynthesis of C(35) terpenes, we carried out functional analyses of three Z-prenyltransferase homologues in M. vanbaalenii identified by genomic analysis. Mvan_3822, a novel bifunctional Z-prenyltransferase, biosynthesizes C(35)-heptaprenyl diphosphate as a main product from (E,E)-farnesyl diphosphate (E,E-FPP) and (E,E,E)-geranylgeranyl diphosphate (E,E,E-GGPP), but produces a C(50)-decaprenyl diphosphate from geranyl diphosphate. Mvan_1705 is a novel Z,E,E-GGPP synthase. In addition, novel cyclic C(35) terpenes, (14E)- and (14Z)-dehydroheptaprenylcycline, were identified as minor metabolites in nonpathogenic Mycobacterium cells. C(35) terpenes could be biosynthesized by two routes, in which E and Z geometric isomers of heptaprenyl diphosphate are produced from E,E-FPP and E,E,E-GGPP, and the prenylreductase responsible for the biosynthesis of C(35) terpenes could reduce both E and Z prenyl residues.
Volume 11(13)
Pages 1874-81
Published 2010-9-3
DOI 10.1002/cbic.201000328
PMID 20672281
MeSH Cyclization Dimethylallyltranstransferase / classification Dimethylallyltranstransferase / genetics Dimethylallyltranstransferase / metabolism* Mycobacterium / enzymology* Recombinant Proteins / classification Recombinant Proteins / isolation & purification Recombinant Proteins / metabolism Stereoisomerism Substrate Specificity Terpenes / chemistry* Terpenes / isolation & purification Terpenes / metabolism*
IF 2.641
Times Cited 9
WOS Category CHEMISTRY, MEDICINAL BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
General Microbes JCM 7439 JCM 13017