Ontology highlight
ABSTRACT:
SUBMITTER: Xie X
PROVIDER: S-EPMC4775309 | biostudies-literature | 2016 Mar
REPOSITORIES: biostudies-literature
Xie Xinqiang X Garg Ashish A Keatinge-Clay Adrian T AT Khosla Chaitan C Cane David E DE
Biochemistry 20160212 8
The role of the conserved active site tyrosine and serine residues in epimerization catalyzed by polyketide synthase ketoreductase (PKS KR) domains has been investigated. Both mutant and wild-type forms of epimerase-active KR domains, including the intrinsically redox-inactive EryKR3° and PicKR3° as well as redox-inactive mutants of EryKR1, were incubated with [2-(2)H]-(2R,3S)-2-methyl-3-hydroxypentanoyl-SACP ([2-(2)H]-2) and 0.05 equiv of NADP(+) in the presence of the redox-active, epimerase-i ...[more]