Open AccessTowards the characterization of squalene synthase activity in extracts of Zymomonas mobilis
Author(s) -
Koukkou Anna I.,
Drainas Constantin,
Rohmer Michel
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08349.x
Subject(s) - squalene , zymomonas mobilis , atp synthase , farnesyl diphosphate farnesyltransferase , chemistry , biochemistry , terpene , biosynthesis , terpenoid , enzyme , stereochemistry , ethanol , prenylation , farnesyltransferase , ethanol fuel
Extracts of Zymomonas mobilis in the presence of NADPH converted tritium‐labelled farnesyl diphosphate (FPP) into squalene, resulting from the activity of squalene synthase, as well as diploptene and diplopterol, derived from further squalene cyclisation. An unidentified isoprenoid representing up to 70% of the conversion products of FPP and different from presqualene alcohol was also formed, even in the absence of NADPH. Addition of squalestatin 1, an inhibitor of squalene synthase, blocked biosynthesis from FPP of the three former triterpenes, in accordance with the role of squalene synthase in their formation, as well as that of the unknown compound.