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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ma, Xiao-xiao Bao, Zhang-zhi Xia, Qingyou Li, Wei-fang Guo, Peng-chao |
| Description | Author Affiliation: Guo PC ( State Key Laboratory of Silkworm Genome Biology, Southwest University, 216, Tiansheng Road, Beibei, Chongqing 400716, People's Republic of China); Bao ZZ ( Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.); Ma XX ( Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.); Xia Q ( State Key Laboratory of Silkworm Genome Biology, Southwest University, 216, Tiansheng Road, Beibei, Chongqing 400716, People's Republic of China.); Li WF ( Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China. Electronic address: liwf@ustc.edu.cn.) |
| Abstract | Saccharomyces cerevisiae Gre2 ( EC1.1.1.283 ) serves as a versatile enzyme that catalyzes the stereoselective reduction of a broad range of substrates including aliphatic and aromatic ketones, diketones, as well as aldehydes, using NADPH as the cofactor. Here we present the crystal structures of Gre2 from S. cerevisiae in an apo-form at 2.00 Å and NADPH-complexed form at 2.40 Å resolution. Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate. Computational simulation combined with site-directed mutagenesis and enzymatic activity analysis enabled us to define a potential substrate-binding pocket that determines the stringent substrate stereoselectivity for catalysis. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 9 |
| Volume Number | 1844 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2014-09-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Apoenzymes Chemistry Coenzymes NADP Oxidoreductases Protein Subunits Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Amino Acid Sequence Genetics Metabolism Crystallography, X-Ray Kinetics Molecular Docking Simulation Molecular Sequence Data Mutagenesis, Site-Directed Protein Binding Protein Multimerization Recombinant Proteins Enzymology Sequence Alignment Substrate Specificity Thermodynamics Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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