Distinct roles of an ionic interaction holding an alpha-helix with catalytic Asp and a beta-strand with catalytic His in a hyperthermophilic esterase EstE1 and a mesophilic esterase rPPE.

Dachuri, VinayKumar; Truongvan, Ngoc; DangThu, Quynh; Jang, Sei-Heon; Lee, ChangWoo

Dachuri, VinayKumar; Truongvan, Ngoc; DangThu, Quynh; Jang, Sei-Heon; Lee, ChangWoo.

Afiliação

Dachuri V; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, 38453, South Korea.
Truongvan N; Research Center for Herbal Convergence on Liver Disease, Daegu Haany University, Gyeongsan, 38578, South Korea.
DangThu Q; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, 38453, South Korea.
Jang SH; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, 38453, South Korea.
Lee C; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, 38453, South Korea.

Extremophiles ; 23(6): 649-657, 2019 Nov.

Article em En | MEDLINE | ID: mdl-31332517

Assuntos

Esterases; Estrutura Secundária de Proteína; Pseudomonas; Proteínas de Bactérias/química; Proteínas de Bactérias/genética; Catálise; Esterases/química; Esterases/genética; Pseudomonas/enzimologia; Pseudomonas/genética

Palavras-chave

Catalytic-site thermal stability; Conformational flexibility; Ionic interaction; Mesophilic esterase; Thermophilic esterase

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Pseudomonas / Estrutura Secundária de Proteína / Esterases Idioma: En Ano de publicação: 2019 Tipo de documento: Article

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