Y
Yingchun Li
Researcher at Texas A&M University
Publications - 16
Citations - 883
Yingchun Li is an academic researcher from Texas A&M University. The author has contributed to research in topics: Active site & Catalysis. The author has an hindex of 15, co-authored 15 publications receiving 826 citations.
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Journal ArticleDOI
Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase.
TL;DR: A mechanism for the hydrolysis of organophosphates by the bacterial PTE has been proposed and is consistent with the existence of a proton relay from Asp301 to His254 to Asp233 that is used to ferry protons away from the active site with substrates that do not require activation of the leaving group phenol.
Journal ArticleDOI
Predicting substrates by docking high-energy intermediates to enzyme structures.
Johannes C. Hermann,Eman Ghanem,Yingchun Li,Frank M. Raushel,John J. Irwin,Brian K. Shoichet +5 more
TL;DR: A method to predict substrates for enzymes of known structure by docking high-energy intermediate forms of the potential substrates by docking KEGG metabolites, which improved the discrimination between decoys and substrates significantly over the corresponding standard ground-state database.
Journal ArticleDOI
Stereoselective Hydrolysis of Organophosphate Nerve Agents by the Bacterial Phosphotriesterase
Ping Chuan Tsai,Andrew N. Bigley,Yingchun Li,Eman Ghanem,C. Linn Cadieux,Shane A. Kasten,Tony E. Reeves,Douglas M. Cerasoli,Frank M. Raushel +8 more
TL;DR: A series of enantiomerically pure chiral nerve agent analogues containing the relevant phosphoryl centers found in GB, GD, GF, VX, and VR has been developed and accurately predicts the improved activity and stereoselectivity against the authentic nerve agents used in this study.
Journal ArticleDOI
Characterization of a phosphodiesterase capable of hydrolyzing EA 2192, the most toxic degradation product of the nerve agent VX
TL;DR: The ability of GpdQ to hydrolyze the phosphonate monoesters provides an alternative selection strategy in the search of enhanced variants of the bacterial phosphotriesterase (PTE) for the hydrolysis of organophosphonate nerve agents.
Journal ArticleDOI
Mechanism of the dihydroorotase reaction
TL;DR: The X-ray crystal structure of DHO showed that the exocyclic alpha-carboxylate of dihydroorotate is bound to the protein via electrostatic interactions with Arg-20, Asn-44, and His-254, indicating that these residues are critical for substrate recognition.