Cargando…
Dynamic Mechanism of Proton Transfer in Mannitol 2-Dehydrogenase from Pseudomonas fluorescens: MOBILE GLU(292) CONTROLS PROTON RELAY THROUGH A WATER CHANNEL THAT CONNECTS THE ACTIVE SITE WITH BULK SOLVENT
The active site of mannitol 2-dehydrogenase from Pseudomonas fluorescens (PfM2DH) is connected with bulk solvent through a narrow protein channel that shows structural resemblance to proton channels utilized by redox-driven proton pumps. A key element of the PfM2DH channel is the “mobile” Glu(292),...
Autores principales: | Klimacek, Mario, Brunsteiner, Michael, Nidetzky, Bernd |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3307286/ https://www.ncbi.nlm.nih.gov/pubmed/22194597 http://dx.doi.org/10.1074/jbc.M111.289223 |
Ejemplares similares
-
Structural and Kinetic Evidence That Catalytic Reaction of Human UDP-glucose 6-Dehydrogenase Involves Covalent Thiohemiacetal and Thioester Enzyme Intermediates
por: Egger, Sigrid, et al.
Publicado: (2012) -
Structure and Mechanism of Human UDP-glucose 6-Dehydrogenase
por: Egger, Sigrid, et al.
Publicado: (2011) -
Structure and Mechanism of Human UDP-xylose Synthase: EVIDENCE FOR A PROMOTING ROLE OF SUGAR RING DISTORTION IN A THREE-STEP CATALYTIC CONVERSION OF UDP-GLUCURONIC ACID
por: Eixelsberger, Thomas, et al.
Publicado: (2012) -
The Relay/Converter Interface Influences Hydrolysis of ATP by Skeletal Muscle Myosin II
por: Bloemink, Marieke J., et al.
Publicado: (2016) -
Cellulases Dig Deep: IN SITU OBSERVATION OF THE MESOSCOPIC STRUCTURAL DYNAMICS OF ENZYMATIC CELLULOSE DEGRADATION
por: Bubner, Patricia, et al.
Publicado: (2012)