title: Specificity of the ester bond forming condensation enzyme SgcC5 in C-1027 biosynthesis.
abstract: 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 catalyze their regio- and stereospecific ester bond formations.
authors.affiliation: Division of Pharmaceutical Sciences, University of Wisconsin-Madison, Madison, Wisconsin 53705, United States.
authors.forename: Shuangjun
authors.initials: S
authors.lastname: Lin
authors.forename: Tingting
authors.initials: T
authors.lastname: Huang
authors.forename: Geoff P
authors.initials: GP
authors.lastname: Horsman
authors.forename: Sheng-Xiong
authors.initials: SX
authors.lastname: Huang
authors.forename: Xun
authors.initials: X
authors.lastname: Guo
authors.forename: Ben
authors.initials: B
authors.lastname: Shen
mesh_terms: D000617:Aminoglycosides / Q000096:biosynthesis* / Q000737:chemistry; D002384:Catalysis; D002950:Citrate (si)-Synthase; D020650:Combinatorial Chemistry Techniques; D053281:Enediynes / Q000737:chemistry; D015394:Molecular Structure; D010453:Peptide Synthases / Q000378:metabolism*; D013237:Stereoisomerism
chemical_list: D000617:Aminoglycosides; D053281:Enediynes; C058024:C 1027; D002950:Citrate (si)-Synthase; D010453:Peptide Synthases; C104385:non-ribosomal peptide synthase