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Discovery of a new flavin N5-adduct in a tyrosine to phenylalanine variant of d-Arginine dehydrogenase.
Iyer, Archana; Reis, Renata A G; Agniswamy, Johnson; Weber, Irene T; Gadda, Giovanni.
Afiliación
  • Iyer A; Department of Chemistry, Georgia State University, Atlanta, GA, 30302, USA.
  • Reis RAG; Department of Chemistry, Georgia State University, Atlanta, GA, 30302, USA.
  • Agniswamy J; Department of Biology, Georgia State University, Atlanta, GA, 30302, USA.
  • Weber IT; Department of Chemistry, Georgia State University, Atlanta, GA, 30302, USA; Department of Biology, Georgia State University, Atlanta, GA, 30302, USA.
  • Gadda G; Department of Chemistry, Georgia State University, Atlanta, GA, 30302, USA; Department of Biology, Georgia State University, Atlanta, GA, 30302, USA; Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA, 30302, USA. Electronic address: ggadda@gsu.edu.
Arch Biochem Biophys ; 715: 109100, 2022 01 15.
Article en En | MEDLINE | ID: mdl-34864048
d-Arginine dehydrogenase from Pseudomonas aeruginosa (PaDADH) catalyzes the flavin-dependent oxidation of d-arginine and other d-amino acids. Here, we report the crystal structure at 1.29 Å resolution for PaDADH-Y249F expressed and co-crystallized with d-arginine. The overall structure of PaDADH-Y249F resembled PaDADH-WT, but the electron density for the flavin cofactor was ambiguous, suggesting the presence of modified flavins. Electron density maps and mass spectrometric analysis confirmed the presence of both N5-(4-guanidino-oxobutyl)-FAD and 6-OH-FAD in a single crystal of PaDADH-Y249F and helped with the further refinement of the X-ray crystal structure. The versatility of the reduced flavin is apparent in the PaDADH-Y249F structure and is evidenced by the multiple functions it can perform in the same active site.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Flavina-Adenina Dinucleótido / Aminoácido Oxidorreductasas / Guanidinas Idioma: En Revista: Arch Biochem Biophys Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Flavina-Adenina Dinucleótido / Aminoácido Oxidorreductasas / Guanidinas Idioma: En Revista: Arch Biochem Biophys Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos