Insights into the FMNAT Active Site of FAD Synthase: Aromaticity is Essential for Flavin Binding and Catalysis.

Serrano, Ana; Arilla-Luna, Sonia; Medina, Milagros

Serrano, Ana; Arilla-Luna, Sonia; Medina, Milagros.

Afiliação

Serrano A; Department of Biochemistry and Molecular and Cellular Biology, Faculty of Sciences, and Institute of Biocomputation and Physics of Complex Systems (Joint Units: BIFI-IQFR and GBsC-CSIC), University of Zaragoza, E-50009 Zaragoza, Spain.
Arilla-Luna S; Centro de Investigaciones Biológicas Margarita Salas, CSIC, Ramiro de Maeztu 9, E-28040 Madrid, Spain.
Medina M; Department of Biochemistry and Molecular and Cellular Biology, Faculty of Sciences, and Institute of Biocomputation and Physics of Complex Systems (Joint Units: BIFI-IQFR and GBsC-CSIC), University of Zaragoza, E-50009 Zaragoza, Spain.

Int J Mol Sci ; 21(10)2020 May 25.

Article em En | MEDLINE | ID: mdl-32466340

Assuntos

Proteínas de Bactérias/química; Domínio Catalítico; Nucleotidiltransferases/química; Proteínas de Bactérias/genética; Proteínas de Bactérias/metabolismo; Corynebacterium/enzimologia; Dinitrocresóis/química; Dinitrocresóis/metabolismo; Interações Hidrofóbicas e Hidrofílicas; Mutação; Nucleotidiltransferases/genética; Nucleotidiltransferases/metabolismo; Fenilalanina/química; Ligação Proteica; Tirosina/química

Palavras-chave

aromatic residues; binding; eukaryotic ATP:FMN:adenylyltransferase; flavin biosynthesis; isoalloxazine; isothermal titration calorimetry; prokaryotic FAD synthase; rational mutagenesis; steady-state kinetics

Texto completo

Imprimir

XML

PubMed Links

Buscar no Google

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Domínio Catalítico / Nucleotidiltransferases Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo

Imprimir

XML

PubMed Links

Buscar no Google