Auto- and Hetero-Catalytic Processing of the N-Terminal Propeptide Promotes the C-Terminal Fibronectin Type III Domain-Mediated Dimerization of a Thermostable Vpr-like Protease.

Huang, Qianqian; Zhang, Kui; Li, Yu; Gan, Fei; Tang, Xiao-Feng; Tang, Bing

Huang, Qianqian; Zhang, Kui; Li, Yu; Gan, Fei; Tang, Xiao-Feng; Tang, Bing.

Afiliação

Huang Q; State Key Laboratory of Virology, College of Life Sciences, Wuhan Universitygrid.49470.3e, Wuhan, China.
Zhang K; State Key Laboratory of Virology, College of Life Sciences, Wuhan Universitygrid.49470.3e, Wuhan, China.
Li Y; State Key Laboratory of Virology, College of Life Sciences, Wuhan Universitygrid.49470.3e, Wuhan, China.
Gan F; Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan Universitygrid.49470.3e, Wuhan, China.
Tang XF; Hubei Provincial Cooperative Innovation Center of Industrial Fermentation, Wuhan, China.
Tang B; Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan Universitygrid.49470.3e, Wuhan, China.

Appl Environ Microbiol ; 88(21): e0150322, 2022 11 08.

Article em En | MEDLINE | ID: mdl-36250702

Assuntos

Domínio de Fibronectina Tipo III; Peptídeo Hidrolases; Peptídeo Hidrolases/metabolismo; Dimerização; Endopeptidases/metabolismo; Subtilisina

Palavras-chave

fibronectin type III domain; maturation; oligomerization; protease-associated domain; serine protease; subtilisin; thermostability

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeo Hidrolases / Domínio de Fibronectina Tipo III Idioma: En Revista: Appl Environ Microbiol Ano de publicação: 2022 Tipo de documento: Article

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