Kinetic, Dynamic, Ligand Binding Properties, and Structural Models of a Dual-Substrate Specific Nudix Hydrolase from Schizosaccharomyces pombe
Author:
Affiliation:
1. Department of Biochemistry, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, Texas 78229-3900
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi802266g
Reference68 articles.
1. The Pfam protein families database
2. The MutT Proteins or “Nudix” Hydrolases, a Family of Versatile, Widely Distributed, “Housecleaning” Enzymes
3. The Nudix hydrolase superfamily
4. The Diadenosine Hexaphosphate Hydrolases fromSchizosaccharomyces pombe and Saccharomyces cerevisiae Are Homologues of the Human Diphosphoinositol Polyphosphate Phosphohydrolase
5. The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif
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2. Substrate ambiguity among the nudix hydrolases: biologically significant, evolutionary remnant, or both?;Cellular and Molecular Life Sciences;2012-11-27
3. Structure based prediction of functional sites with potential Inhibitors to Nudix enzymes from disease causing microbes;Bioinformation;2011-01-22
4. Current awareness on yeast;Yeast;2010-01
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