Crystal structure of native ß-N-acetylhexosaminidase isolated from Aspergillus oryzae sheds light onto its substrate specificity, high stability, and regulation by propeptide.

Skerlová, Jana; Bláha, Jan; Pachl, Petr; Hofbauerová, Katerina; Kukacka, Zdenek; Man, Petr; Pompach, Petr; Novák, Petr; Otwinowski, Zbyszek; Brynda, Jirí; Vanek, Ondrej; Rezácová, Pavlína

Crystal structure of native ß-N-acetylhexosaminidase isolated from Aspergillus oryzae sheds light onto its substrate specificity, high stability, and regulation by propeptide.

Skerlová, Jana; Bláha, Jan; Pachl, Petr; Hofbauerová, Katerina; Kukacka, Zdenek; Man, Petr; Pompach, Petr; Novák, Petr; Otwinowski, Zbyszek; Brynda, Jirí; Vanek, Ondrej; Rezácová, Pavlína.

Afiliação

Skerlová J; Institute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.
Bláha J; Institute of Molecular Genetics, The Czech Academy of Sciences, Prague, Czech Republic.
Pachl P; Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic.
Hofbauerová K; Institute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.
Kukacka Z; Institute of Microbiology, The Czech Academy of Sciences, Prague, Czech Republic.
Man P; Institute of Physics, Faculty of Mathematics and Physics, Charles University, Prague, Czech Republic.
Pompach P; Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic.
Novák P; Institute of Microbiology, The Czech Academy of Sciences, Prague, Czech Republic.
Otwinowski Z; Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic.
Brynda J; Institute of Microbiology, The Czech Academy of Sciences, Prague, Czech Republic.
Vanek O; Institute of Microbiology, The Czech Academy of Sciences, Prague, Czech Republic.
Rezácová P; Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic.

FEBS J ; 285(3): 580-598, 2018 02.

Article em En | MEDLINE | ID: mdl-29239122

Assuntos

Aspergillus oryzae/enzimologia; Proteínas Fúngicas/metabolismo; Proteína Ativadora de G(M2)/metabolismo; Gangliosídeo G(M2)/metabolismo; Modelos Moleculares; beta-N-Acetil-Hexosaminidases/metabolismo; Sequência de Aminoácidos; Sítios de Ligação; Domínio Catalítico; Sequência Conservada; Cristalografia por Raios X; Dimerização; Precursores Enzimáticos/química; Precursores Enzimáticos/metabolismo; Proteínas Fúngicas/química; Proteína Ativadora de G(M2)/química; Gangliosídeo G(M2)/química; Glicosilação; Ligantes; Domínios e Motivos de Interação entre Proteínas; Processamento de Proteína Pós-Traducional; Estabilidade Proteica; Alinhamento de Sequência; Homologia Estrutural de Proteína; Especificidade por Substrato; beta-N-Acetil-Hexosaminidases/química

Palavras-chave

X-ray crystallography; active pocket; carbohydrate biotechnology; glycosylation; mass spectrometry; propeptide

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Aspergillus oryzae / Beta-N-Acetil-Hexosaminidases / Proteínas Fúngicas / Modelos Moleculares / Proteína Ativadora de G(M2) / Gangliosídeo G(M2) Idioma: En Ano de publicação: 2018 Tipo de documento: Article

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