220654-32-0Relevant academic research and scientific papers
Seven-enzyme in vitro cascade to (3R)-3-hydroxybutyryl-CoA
Valencia, Luis E.,Zhang, Zhicheng,Cepeda, Alexis J.,Keatinge-Clay, Adrian T.
, p. 1375 - 1378 (2019)
Economical and environmentally-friendly routes to convert feedstock chemicals like acetate into valuable chiral products such as (R)-3-hydroxybutyrate are in demand. Here, seven enzymes (CoaA, CoaD, CoaE, ACS, BktB, PhaB, and GDH) are employed in a one-pot, in vitro, biocatalytic synthesis of (3R)-3-hydroxybutyryl-CoA, which was readily isolated. This platform generates not only chiral diketide building blocks but also desirable CoA derivatives.
In vitro kinetic study of the squalestatin tetraketide synthase dehydratase reveals the stereochemical course of a fungal highly reducing polyketide synthase
Liddle, Emma,Scott, Alan,Han, Li-Chen,Ivison, David,Simpson, Thomas J.,Willis, Christine L.,Cox, Russell J.
supporting information, p. 1727 - 1730 (2017/02/10)
Six potential diketide substrates for the squalestatin tetraketide synthase (SQTKS) dehydratase (DH) domain were synthesised as N-acetyl cysteamine thiolesters (SNAC) and tested in kinetic assays as substrates with an isolated DH domain. 3R-3-hydroxybutyryl SNAC 3R-16 was turned over by the enzyme, but its enantiomer was not. Of the four 2-methyl substrates only 2R,3R-2-methyl-3-hydroxybutyryl SNAC 2R,3R-8 was a substrate. Combined with stereochemical information from the isolated SQTKS enoyl reductase (ER) domain, our results provide a near complete stereochemical description of the first cycle of beta-modification reactions of a fungal highly reducing polyketide synthase (HR-PKS). The results emphasise the close relationship between fungal HR-PKS and vertebrate fatty acid synthases (vFAS).
Enediyne polyketide synthases stereoselectively reduce the β-ketoacyl intermediates to β- D -hydroxyacyl intermediates in enediyne core biosynthesis
Ge, Hui-Ming,Huang, Tingting,Rudolf, Jeffrey D.,Lohman, Jeremy R.,Huang, Sheng-Xiong,Guo, Xun,Shen, Ben
supporting information, p. 3958 - 3961 (2014/08/18)
PKSE biosynthesizes an enediyne core precursor from decarboxylative condensation of eight malonyl-CoAs. The KR domain of PKSE is responsible for iterative β-ketoreduction in each round of polyketide chain elongation. KRs from selected PKSEs were investiga
