Xuelian Du

Works (2)

Updated: July 5th, 2023 15:56

2010 journal article

Improving the catalytic activity of hyperthermophilic Pyrococcus prolidases for detoxification of organophosphorus nerve agents over a broad range of temperatures

Applied Microbiology and Biotechnology, 87(5), 1715–1726.

By: C. Theriot n, X. Du n, S. Tove n & A. Grunden n 

author keywords: Prolidase; Pyrococcus furiosus; OP nerve agents; Mutagenesis; Directed evolution
MeSH headings : Amino Acid Substitution / genetics; Archaeal Proteins / chemistry; Archaeal Proteins / genetics; Archaeal Proteins / isolation & purification; Archaeal Proteins / metabolism; Chemical Warfare Agents / metabolism; Culture Media / chemistry; Dipeptidases / chemistry; Dipeptidases / genetics; Dipeptidases / isolation & purification; Dipeptidases / metabolism; Enzyme Stability; Escherichia coli / genetics; Models, Molecular; Mutagenesis; Organophosphorus Compounds / metabolism; Pesticides / metabolism; Plasmids; Polymerase Chain Reaction / methods; Protein Stability; Protein Structure, Tertiary; Pyrococcus furiosus / enzymology; Pyrococcus furiosus / genetics; Sequence Deletion; Temperature
topics (OpenAlex): Peptidase Inhibition and Analysis; Neuropeptides and Animal Physiology; Protease and Inhibitor Mechanisms
TL;DR: To obtain a better enzyme for OP nerve agent decontamination and to investigate structural factors that influence protein thermostability and thermoactivity, randomly mutated P. furiosus prolidase mutants with improved activity over a broader range of temperatures were isolated. (via Semantic Scholar)
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Sources: Web Of Science, Crossref, NC State University Libraries
Added: August 6, 2018

2005 article

Characterization of the dinuclear metal center of Pyrococcus furiosus prolidase by analysis of targeted mutants

Du, X., Tove, S., Kast-Hutcheson, K., & Grunden, A. M. (2005, October 11). FEBS Letters, Vol. 579, pp. 6140–6146.

By: X. Du n, S. Tove*, K. Kast-Hutcheson n & A. Grunden n 

author keywords: prolidase; aminopeptidase; dinuclear metal center; cobalt enzyme; Pyrococcus furiosus
MeSH headings : Archaeal Proteins / chemistry; Archaeal Proteins / genetics; Binding Sites; Catalysis; Cobalt / chemistry; Dipeptidases / chemistry; Dipeptidases / genetics; Mutation; Pyrococcus furiosus / enzymology
topics (OpenAlex): Peptidase Inhibition and Analysis; Neuropeptides and Animal Physiology; Protease and Inhibitor Mechanisms
TL;DR: Metal‐content, enzyme activity and CD‐spectra analyses of D209A‐, H284L‐, and E327L‐prolidase mutants show that Co1 is the tight‐binding and Co2 the loose‐binding metal center. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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