103273-05-8Relevant academic research and scientific papers
The CYPome of sorangium cellulosum so ce56 and identification of CYP109D1 as a new fatty acid hydroxylase
Khatri, Yogan,Hannemann, Frank,Ewen, Kerstin M.,Pistorius, Dominik,Perlova, Olena,Kagawa, Norio,Brachmann, Alexander O.,Mueller, Rolf,Bernhardt, Rita
, p. 1295 - 1305 (2010)
The first systematic study of the complete cytochrome P450 complement (CYPome) of Sorangium cellulosum So ce56, which is a producer of important secondary metabolites and has the largest bacterial genome sequenced to date, is presented. We describe the bioinformatic analysis of the So ce56 cytochrome P450 complement consisting of 21 putative P450 genes. Because fatty acids play a pivotal role during the complex life cycle of myxobacteria, we focused our studies on the characterization of fatty acid hydroxylases. Three novel potential fatty acid hydroxylases (CYP109D1, CYP264A1, and CYP266A1) were used for detailed characterization. One of them, CYP109D1 was able to perform subterminal hydroxylation of saturated fatty acids with the support of two autologous and one heterologous electron transfer system(s). The kinetic parameters for the product hydroxylation were derived.
The self-sufficient CYP102 family enzyme, Krac9955, from Ktedonobacter racemifer DSM44963 acts as an alkyl- and alkyloxy-benzoic acid hydroxylase
Maddigan, Natasha K.,Bell, Stephen G.
, p. 15 - 21 (2017/01/10)
A self-sufficient CYP102 family encoding gene (Krac_9955) has been identified from the bacterium Ktedonobacter racemifer DSM44963 which belongs to the Chloroflexi phylum. The characterisation of the substrate range of this enzyme was hampered by low levels of production using E. coli. The yield and purity of the Krac9555 enzyme was improved using a codon optimised gene, the introduction of a tag and modification of the purification protocol. The heme domain was isolated and in?vitro analysis of substrate binding and turnover was performed. Krac9955 was found to preferentially bind alkyl- and alkyloxy-benzoic acids (≥95% high spin, Kd?a self-sufficient CYP102 family member Krac9955 showed low levels of NAD(P)H oxidation activity for all the substrates tested though product formation was observed for many. For nearly all substrates the preferred site of hydroxylation of Krac9955 was eight carbons away from the carboxylate group with certain reactions proceeding at ≥ 90% selectivity. Krac9955 differs from CYP102A1 (P450Bm3), and is the first self-sufficient member of the CYP102 family of P450 enzymes which is not optimised for fast fatty acid hydroxylation close to the ω-terminus.
Regioselectivity and Activity of Cytochrome P450 BM-3 and Mutant F87A in Reactions Driven by Hydrogen Peroxide
Cirino, Patrick C.,Arnold, Frances H.
, p. 932 - 937 (2007/10/03)
Cytochrome P450 BM-3 (EC 1.14.14.1) is a monooxygenase that utilizes NADPH and dioxygen to hydroxylate fatty acids at subterminal positions. The enzyme is also capable of functioning as a peroxygenase in the same reaction, by utilizing hydrogen peroxide i
An efficient synthesis of open chain nitroalcohols by regioselective ring opening of cyclic tert-β-nitroalcohols by sodium borohydride: Short synthesis of (±)-tridecan-12-olide and (±)-9-tetradecanolide
Bez, Ghanashyam,Saikia, Anil K.,Kalita, Dipak,Bezbarua, Maitreyee S.,Barua, Nabin G.
, p. 325 - 330 (2007/10/03)
It has been demonstrated that a wide variety of cyclic tert-β-nitroalcohols can be efficiently cleaved regioselectively using stoichiometric amount of NaBH4 in organic solvents like dry MeOH, Et2O, CH3CN etc. giving open c
