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ACS Chem Biol. 2015 Sep 18;10(9):2048-56. doi: 10.1021/acschembio.5b00244. Epub 2015 Jun 23.

Structural Basis for the Stereochemical Control of Amine Installation in Nucleotide Sugar Aminotransferases.

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Center for Pharmaceutical Research and Innovation, University of Kentucky College of Pharmacy , 789 South Limestone Street, Lexington, Kentucky 40536-0596, United States ;
Department of Biochemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.


Sugar aminotransferases (SATs) are an important class of tailoring enzymes that catalyze the 5'-pyridoxal phosphate (PLP)-dependent stereo- and regiospecific installation of an amino group from an amino acid donor (typically L-Glu or L-Gln) to a corresponding ketosugar nucleotide acceptor. Herein we report the strategic structural study of two homologous C4 SATs (Micromonospora echinospora CalS13 and Escherichia coli WecE) that utilize identical substrates but differ in their stereochemistry of aminotransfer. This study reveals for the first time a new mode of SAT sugar nucleotide binding and, in conjunction with previously reported SAT structural studies, provides the basis from which to propose a universal model for SAT stereo- and regiochemical control of amine installation. Specifically, the universal model put forth highlights catalytic divergence to derive solely from distinctions within nucleotide sugar orientation upon binding within a relatively fixed SAT active site where the available ligand bound structures of the three out of four representative C3 and C4 SAT examples provide a basis for the overall model. Importantly, this study presents a new predictive model to support SAT functional annotation, biochemical study and rational engineering.

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