33758-16-6Relevant articles and documents
Optimized Reaction Conditions Enable the Hydration of Non-natural Substrates by the Oleate Hydratase from Elizabethkingia meningoseptica
Demming, Rebecca M.,Otte, Konrad B.,Nestl, Bettina M.,Hauer, Bernhard
, p. 758 - 766 (2017)
The oleate hydratase from Elizabethkingia meningoseptica (Em-OAH) catalyzes the hydration of oleic acid (C18) to (R)-10-hydroxystearic acid. In previous work, low activity of Em-OAH towards chemically synthesized (Z)-undec-9-enoic acid (C11) was observed. Product formation in the hydration of the truncated C11 substrate was improved by optimizing the reaction conditions by applying statistical experiment design. Optimized reaction conditions resulted in a 2.8-fold increase in product formation in just one quarter of the time (64 % conversion in 28 h). The applicability has been assessed in the upscaling of the conversion of (Z)-undec-9-enoic acid to (S)-10-hydroxyundecanoic acid (132 mg product, >95 % purity). Reaction conditions developed for the hydration of C11 facilitated the first hydration of non-natural alkenes. By using a fatty acid dummy substrate, 1-decene was successfully hydrated to (S)-2-decanol with excellent stereoselectivity and 50 % conversion after four days of incubation.
Identification of a Robust Carbonyl Reductase for Diastereoselectively Building syn-3,5-Dihydroxy Hexanoate: A Bulky Side Chain of Atorvastatin
Gong, Xu-Min,Zheng, Gao-Wei,Liu, You-Yan,Xu, Jian-He
supporting information, p. 1349 - 1354 (2017/09/23)
t-Butyl-6-cyano-(3R,5R)-dihydroxyhexanoate is an advanced chiral precursor for the synthesis of the side chain pharmacophore of cholesterol-lowering drug atorvastatin. Herein, a robust carbonyl reductase (LbCR) was newly identified from Lactobacillus brevis, which displays high activity and excellent diastereoselectivity toward bulky t-butyl 6-cyano-(5R)-hydroxy-3-oxo-hexanoate (7). The engineered Escherichia coli cells harboring LbCR and glucose dehydrogenase (for cofactor regeneration) were employed as biocatalysts for the asymmetric reduction of substrate 7. As a result, as much as 300 g L-1 of water-insoluble substrate was completely converted to the corresponding chiral diol with >99.5% de in a space-time yield of 351 g L-1 d-1, indicating a great potential of LbCR for practical synthesis of the very bulky and bi-chiral 3,5-dihydroxy carboxylate side chain of best-selling statin drugs.
A novel P450-based biocatalyst for the selective production of chiral 2-alkanols
Von Bühler, Clemens J.,Urlacher, Vlada B.
supporting information, p. 4089 - 4091 (2014/04/03)
A P450 monooxygenase from Nocardia farcinica (CYP154A8) catalyses the stereo- and regioselective hydroxylation of n-alkanes, still a challenging task in chemical catalysis. In a biphasic reaction system, the regioselectivity for the C2-position of C7-C9 alkanes was over 90%. The enzyme showed strict S-selectivity for all tested substrates, with enantiomeric excess (ee) of up to 91%. This journal is the Partner Organisations 2014.