Weiling Niu
Saint Louis University
11 Papers
180 Citations
Weiling Niu is an academic researcher from Saint Louis University. The author has contributed to research in topics: Isocitrate lyase & Lyase. The author has an hindex of 10, co-authored 11 publications. Previous affiliations of Weiling Niu include University of New Mexico & Washington University in St. Louis.
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Papers
Crystallographic and Kinetic Evidence of Allostery in a Trypsin-like Protease.
Weiling Niu,Zhiwei Chen,Prafull S. Gandhi,Austin D. Vogt,Nicola Pozzi,Leslie A. Pelc,Fatima Zapata,Enrico Di Cera +7 more
TL;DR: In this paper, a structural validation of a pre-existing equilibrium between alternative conformations remains a challenge even for textbook examples of allosteric proteins (e.g., trypsin-like proteins).
Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation.
TL;DR: The first x-ray crystal structure of prothrombin as a Gla-domainless construct carrying an Ala replacement of the catalytic Ser-525 is reported, indicating a structure-based mechanism of prohrombin activation emerges.
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Identification of fungal oxaloacetate hydrolyase within the isocitrate lyase/PEP mutase enzyme superfamily using a sequence marker-based method.
Henk-Jan Joosten,Ying Han,Weiling Niu,Jacques Vervoort,Debra Dunaway-Mariano,Peter J. Schaap +5 more
TL;DR: It is proposed that presence of this serine in family members correlates with presence of OAH activity whereas its absence correlates with absence of OAS, and is tested by carrying out a serine mutagenesis study with the OAH from the fungal oxalic acid producer Botrytis cinerea and the O AH active plant petal death protein as test systems.
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Autoactivation of thrombin precursors.
Nicola Pozzi,Zhiwei Chen,Fatima Zapata,Weiling Niu,Sergio Barranco-Medina,Leslie A. Pelc,Enrico Di Cera +6 more
TL;DR: It is shown that replacement of key residues within the activation domain causes these zymogens to spontaneously convert to thrombin, and a new strategy emerges for the facile production of enzymes through zymogen autoactivation that is broadly applicable to trypsin-like proteases of biotechnological and clinical interest.
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Structure and Kinetics of Phosphonopyruvate Hydrolase from VorioVorax sp. Pal2: New Insight into the Divergence of Catalysis within the PEP Mutase/Isocitrate Lyase Superfamily †,‡
Celia C. H. Chen,Ying Han,Weiling Niu,Anna N. Kulakova,Andrew Howard,John P. Quinn,Debra Dunaway-Mariano,Osnat Herzberg +7 more
TL;DR: The proposed PPH catalytic mechanism is analogous to that of PEPM but includes activation of a water nucleophile with the loop Thr118 residue and may have favored the open conformation of PPH even when the enzyme was cocrystallized with the oxalate inhibitor.