Cargando…
Structural analysis of urate oxidase in complex with its natural substrate inhibited by cyanide: Mechanistic implications
BACKGROUND: Urate oxidase (EC 1.7.3.3 or UOX) catalyzes the conversion of uric acid and gaseous molecular oxygen to 5-hydroxyisourate and hydrogen peroxide, in the absence of cofactor or particular metal cation. The functional enzyme is a homo-tetramer with four active sites located at dimeric inter...
Autores principales: | Gabison, Laure, Prangé, Thierry, Colloc'h, Nathalie, El Hajji, Mohamed, Castro, Bertrand, Chiadmi, Mohamed |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2490695/ https://www.ncbi.nlm.nih.gov/pubmed/18638417 http://dx.doi.org/10.1186/1472-6807-8-32 |
Ejemplares similares
-
Direct Evidence for a Peroxide Intermediate and a Reactive Enzyme–Substrate–Dioxygen Configuration in a Cofactor-free Oxidase**
por: Bui, Soi, et al.
Publicado: (2014) -
Urate Oxidase Purification by Salting-in Crystallization: Towards an Alternative to Chromatography
por: Giffard, Marion, et al.
Publicado: (2011) -
Structural Basis for Xenon Inhibition in a Cationic Pentameric Ligand-Gated Ion Channel
por: Sauguet, Ludovic, et al.
Publicado: (2016) -
The Neutron Structure of Urate Oxidase Resolves a Long-Standing Mechanistic Conundrum and Reveals Unexpected Changes in Protonation
por: Oksanen, Esko, et al.
Publicado: (2014) -
Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography
por: Colloc’h, Nathalie, et al.
Publicado: (2017)