The tetrameric structure of sialic acid-synthesizing UDP-GlcNAc 2-epimerase from <i>Acinetobacter baumannii</i>: A comparative study with human GNE.

Ko, Tzu-Ping; Lai, Shu-Jung; Hsieh, Tung-Ju; Yang, Chia-Shin; Chen, Yeh

The tetrameric structure of sialic acid-synthesizing UDP-GlcNAc 2-epimerase from Acinetobacter baumannii: A comparative study with human GNE.

Ko, Tzu-Ping; Lai, Shu-Jung; Hsieh, Tung-Ju; Yang, Chia-Shin; Chen, Yeh.

Afiliação

Ko TP; From the Institute of Biological Chemistry, Academia Sinica, Taipei 115.
Lai SJ; From the Institute of Biological Chemistry, Academia Sinica, Taipei 115.
Hsieh TJ; the Research Center for Tumor Medical Science, China Medical University, Taichung 404, and.
Yang CS; the Department of Biotechnology, Hungkuang University, Taichung 433, Taiwan.
Chen Y; the Department of Biotechnology, Hungkuang University, Taichung 433, Taiwan chyeah6599@sunrise.hk.edu.tw.

J Biol Chem ; 293(26): 10119-10127, 2018 06 29.

Article em En | MEDLINE | ID: mdl-29764940

Assuntos

Acinetobacter baumannii/enzimologia; Ácido N-Acetilneuramínico/biossíntese; Multimerização Proteica; Carboidratos Epimerases/química; Carboidratos Epimerases/metabolismo; Domínio Catalítico; Sequência Conservada; Humanos; Ligantes; Estrutura Quaternária de Proteína

Palavras-chave

N-acetyl neuraminic acid; catalysis; catalytic mechanism; hydrolase; hydrolytic enzyme; inhibition mechanism; inhibitor; inhibitor design; oligomer; protein crystallization; protein oligomer

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ácido N-Acetilneuramínico / Acinetobacter baumannii / Multimerização Proteica Limite: Humans Idioma: En Revista: J Biol Chem Ano de publicação: 2018 Tipo de documento: Article

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