Insights into the fmnat active site of fad synthase: Aromaticity is essential for flavin binding and catalysis
16 pags., 9 figs., 3 tabs. -- This article belongs to the Special Issue Flavin Adenine Dinucleotide (FAD): Biosynthesis and Function
| Autores: | , , |
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| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2020 |
| País: | España |
| Recursos: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/233588 |
| Acesso em linha: | http://hdl.handle.net/10261/233588 |
| Access Level: | acceso abierto |
| Palavra-chave: | Flavin biosynthesis Prokaryotic FAD synthase Eukaryotic ATP:FMN:adenylyltransferase Aromatic residues Isoalloxazine Binding Rational mutagenesis Isothermal titration calorimetry Steady-state kinetics |
| Resumo: | 16 pags., 9 figs., 3 tabs. -- This article belongs to the Special Issue Flavin Adenine Dinucleotide (FAD): Biosynthesis and Function |
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