OleA is a thiolase superfamily enzyme that has been shown to catalyze the condensation of two long-chain fatty acyl-coenzyme A (CoA) substrates. The enzyme is part of a larger gene cluster responsible for generating long-chain olefin products, a potential biofuel precursor. In thiolase superfamily enzymes, catalysis is achieved via a ping-pong mechanism.
View Article and Find Full Text PDFOleA catalyzes the condensation of fatty acyl groups in the first step of bacterial long-chain olefin biosynthesis, but the mechanism of the condensation reaction is controversial. In this study, OleA from Xanthomonas campestris was expressed in Escherichia coli and purified to homogeneity. The purified protein was shown to be active with fatty acyl-CoA substrates that ranged from C(8) to C(16) in length.
View Article and Find Full Text PDFActa Crystallogr Sect F Struct Biol Cryst Commun
September 2010
OleC, a biosynthetic enzyme involved in microbial hydrocarbon biosynthesis, has been crystallized. Synchrotron X-ray diffraction data have been collected to 3.4 A resolution.
View Article and Find Full Text PDFArthrobacter aurescens TC1, Arthrobacter chlorophenolicus A6, Arthrobacter crystallopoietes, and Arthrobacter oxydans produce long-chain monoalkenes, predominantly cis-3,25-dimethyl-13-heptacosene. Four other Arthrobacter strains did not form alkenes. The level of cis-3,25-dimethyl-13-heptacosene in Arthrobacter chlorophenolicus A6 remained proportional to cell mass during growth.
View Article and Find Full Text PDFVibrio furnissii M1 was recently reported to biosynthesize n-alkanes when grown on biopolymers, sugars, or organic acids (M. O. Park, J.
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