Structure-based redesign of the bacterial prolidase active-site pocket for efficient enhancement of methyl-parathion hydrolysis-Reference-Cited by-同舟云学术

Structure-based redesign of the bacterial prolidase active-site pocket for efficient enhancement of methyl-parathion hydrolysis

Published:2021 Issue: Volume: Page:
ISSN:2044-4753
Container-title:Catalysis Science & Technology
language:en
Short-container-title:Catal. Sci. Technol.

Author:

Yang Jian¹²³⁴⁵^ORCID,Xiao Yunzhu¹²³⁴⁵,Liu Yu¹²³⁴⁵,Li Ru¹²³⁴⁵,Long Lijuan¹²³⁴⁵

Affiliation:

1. CAS Key Laboratory of Tropical Marine Bio-resources and Ecology

2. Guangdong Key Laboratory of Marine Materia Medica

3. South China Sea Institute of Oceanology

4. Chinese Academy of Sciences

5. Guangzhou 510301

Abstract

Mutagenesis at four residues surrounding the active-site pocket of an old bacterial prolidase scaffold led to a 10 000-fold increase in methyl-parathion hydrolysis and broadening substrate specificity against organophosphorus compounds.

Funder

Natural Science Foundation of Guangdong Province

Guangzhou Science and Technology Program key projects

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2021/CY/D1CY00490E

Reference40 articles.

1. Microbial degradation of organophosphorus compounds

2. Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro

3. Early Death Due to Severe Organophosphate Poisoning Is a Centrally Mediated Process

4. Organophosphate and Carbamate Poisoning

5. Enzymatic Bioremediation of Organophosphate Compounds—Progress and Remaining Challenges

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