Structural highlights
Publication Abstract from PubMed
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 2.00A and NADPH-complexed form at 2.40A 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.
Structural insights into the cofactor-assisted substrate recognition of yeast methylglyoxal/isovaleraldehyde reductase Gre2.,Guo PC, Bao ZZ, Ma XX, Xia Q, Li WF Biochim Biophys Acta. 2014 Sep;1844(9):1486-92. doi:, 10.1016/j.bbapap.2014.05.008. Epub 2014 May 27. PMID:24879127[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo PC, Bao ZZ, Ma XX, Xia Q, Li WF. Structural insights into the cofactor-assisted substrate recognition of yeast methylglyoxal/isovaleraldehyde reductase Gre2. Biochim Biophys Acta. 2014 Sep;1844(9):1486-92. doi:, 10.1016/j.bbapap.2014.05.008. Epub 2014 May 27. PMID:24879127 doi:https://dx.doi.org/10.1016/j.bbapap.2014.05.008
