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Microbial phosphotriesterase: structure, function, and biotechnological applications


Citation

Latip, Wahhida and Knight, Victor Feizal and Abdul Halim, Norhana and Ong, Keat Khim and Mohd Kasim, Noor Azilah and Wan Yunus, Wan Md. Zin and Mohd Noor, Siti Aminah and Mohamad Ali, Mohd Shukuri (2019) Microbial phosphotriesterase: structure, function, and biotechnological applications. Catalysts, 9 (8). art. no. 671. pp. 1-11. ISSN 2073-4344

Abstract

The role of phosphotriesterase as an enzyme which is able to hydrolyze organophosphate compounds cannot be disputed. Contamination by organophosphate (OP) compounds in the environment is alarming, and even more worrying is the toxicity of this compound, which affects the nervous system. Thus, it is important to find a safer way to detoxify, detect and recuperate from the toxicity effects of this compound. Phosphotriesterases (PTEs) are mostly isolated from soil bacteria and are classified as metalloenzymes or metal-dependent enzymes that contain bimetals at the active site. There are three separate pockets to accommodate the substrate into the active site of each PTE. This enzyme generally shows a high catalytic activity towards phosphotriesters. These microbial enzymes are robust and easy to manipulate. Currently, PTEs are widely studied for the detection, detoxification, and enzyme therapies for OP compound poisoning incidents. The discovery and understanding of PTEs would pave ways for greener approaches in biotechnological applications and to solve environmental issues relating to OP contamination.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
DOI Number: https://doi.org/10.3390/catal9080671
Publisher: MDPI
Keywords: Phosphotriestease; Structure; Function or reaction; Biotechnological application
Depositing User: Nabilah Mustapa
Date Deposited: 04 May 2020 16:12
Last Modified: 04 May 2020 16:12
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.3390/catal9080671
URI: http://psasir.upm.edu.my/id/eprint/38289
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