Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase-Reference-Cited by-同舟云学术

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Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase

Published:2010-12 Issue:23 Volume:101 Page:9204-9212
ISSN:0960-8524
Container-title:Bioresource Technology
language:en
Short-container-title:Bioresource Technology

Author:

Merone Luigia,Mandrich Luigi,Porzio Elena,Rossi Mosé,Müller Susanne,Reiter Georg,Worek Franz,Manco Giuseppe

Publisher

Elsevier BV

Subject

Waste Management and Disposal,Renewable Energy, Sustainability and the Environment,General Medicine,Environmental Engineering,Bioengineering

Reference35 articles.

1. The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase;Afriat;Biochemistry,2006

2. Latent evolutionary potentials under the neutral mutational drift of an enzyme;Amitai;HFSP J.,2007

3. Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase;Aubert;Biochemistry,2004

4. Protein stability promotes evolvability;Bloom;Proc. Natl. Acad. Sci. USA,2006

5. Alteromonas prolidase for organophosphorous G-agent decontamination;Cheng;Chem. Biol. Interact.,1999

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1. Applications of Microbial Organophosphate-Degrading Enzymes to Detoxification of Organophosphorous Compounds for Medical Countermeasures against Poisoning and Environmental Remediation;International Journal of Molecular Sciences;2024-07-17

2. Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity;JACS Au;2024-04-25

3. Tuning the Envelope Structure of Enzyme Nanoreactors for In Vivo Detoxification of Organophosphates;International Journal of Molecular Sciences;2023-10-30

4. A mesophilic phosphotriesterase-like lactonase shows high stability and proficiency as quorum quenching enzyme;Chemico-Biological Interactions;2023-09

5. Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity;2023-05-22

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