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Specificity of the ester bond forming condensation enzyme SgcC5 in C-1027 biosynthesis.
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ABSTRACT:
SUBMITTER: Lin S
PROVIDER: S-EPMC3345089 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
Publications
Specificity of the ester bond forming condensation enzyme SgcC5 in C-1027 biosynthesis.
Organic letters 20120420 9
The SgcC5 condensation enzyme catalyzes the attachment of SgcC2-tethered (S)-3-chloro-5-hydroxy-β-tyrosine (2) to the enediyne core in C-1027 (1) biosynthesis. It is reported that SgcC5 (i) exhibits high stereospecificity toward the (S)-enantiomers of SgcC2-tethered β-tyrosine and analogues as donors, (ii) prefers the (R)-enantiomers of 1-phenyl-1,2-ethanediol (3) and analogues, mimicking the enediyne core, as acceptors, and (iii) can recognize a variety of donor and acceptor substrates to catal ...[more]