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Disulfide bridge formation to increase thermostability of DFPase enzyme: A computational study.
Mohammadi, Mozafar; Sakhteman, Amirhossein; Ahrari, Sajjad; Hassanpour, Kazem; Hashemi, Sayed Ebrahim; Farnoosh, Gholamreza.
Afiliação
  • Mohammadi M; Applied Biotechnology Research Centre, Baqiyatallah University of Medical Sciences, Tehran, Iran.
  • Sakhteman A; School of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran.
  • Ahrari S; Department of Pharmaceutical Biotechnology, Pharmaceutical Science Research Center, Faculty of Pharmacy, Shiraz University of Medical Sciences, Shiraz, Iran.
  • Hassanpour K; Medical School, Sabzevar University of Medical Sciences, Sabzevar, Iran.
  • Hashemi SE; Exercise Physiology Research Center, Lifestyle Institute, Baqiyatallah University of Medical Sciences, Tehran, Iran.
  • Farnoosh G; Applied Biotechnology Research Centre, Baqiyatallah University of Medical Sciences, Tehran, Iran. Electronic address: Rzfarnoosh@yahoo.com.
Comput Biol Chem ; 77: 272-278, 2018 Dec.
Article em En | MEDLINE | ID: mdl-30396154
ABSTRACT
Organophosphate compounds bioremediation by use of organophosphorus degradation enzymes such as DFPase is a developing interest in industry and medicine. The most important problem with the bio-catalytic enzymes is their instability on high temperatures. This work carried out to find suitable locations for introducing disulfide bridges in DFPase enzyme. We employed some computational approaches to design the disulfide bridges and evaluate their roles in the enzyme structural thermostability. According to the in silico results, mutant 6 (V24C, C76) increased the enzyme thermostability relative to wild-type.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Hidrolases de Triester Fosfórico / Loligo Limite: Animals Idioma: En Revista: Comput Biol Chem Assunto da revista: BIOLOGIA / INFORMATICA MEDICA / QUIMICA Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Irã

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Hidrolases de Triester Fosfórico / Loligo Limite: Animals Idioma: En Revista: Comput Biol Chem Assunto da revista: BIOLOGIA / INFORMATICA MEDICA / QUIMICA Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Irã