Cargando…
Enzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate Isomerase
[Image: see text] Two mutations of the phosphodianion gripper loop in chicken muscle triosephosphate isomerase (cTIM) were examined: (1) the loop deletion mutant (LDM) formed by removal of residues 170–173 [Pompliano, D. L., et al. (1990) Biochemistry 29, 3186–3194] and (2) the loop 6 replacement mu...
Autores principales: | Zhai, Xiang, Go, Maybelle K., O’Donoghue, AnnMarie C., Amyes, Tina L., Pegan, Scott D., Wang, Yan, Loria, J. Patrick, Mesecar, Andrew D., Richard, John P. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4051426/ https://www.ncbi.nlm.nih.gov/pubmed/24825099 http://dx.doi.org/10.1021/bi500458t |
Ejemplares similares
-
Role
of Loop-Clamping Side Chains in Catalysis by
Triosephosphate Isomerase
por: Zhai, Xiang, et al.
Publicado: (2015) -
Enzyme
Architecture: Modeling the Operation of a Hydrophobic
Clamp in Catalysis by Triosephosphate Isomerase
por: Kulkarni, Yashraj S., et al.
Publicado: (2017) -
Enzyme
Architecture: Remarkably Similar Transition
States for Triosephosphate Isomerase-Catalyzed Reactions of the Whole
Substrate and the Substrate in Pieces
por: Zhai, Xiang, et al.
Publicado: (2014) -
Enzyme
Architecture: Amino Acid Side-Chains That Function
To Optimize the Basicity of the Active Site Glutamate of Triosephosphate
Isomerase
por: Zhai, Xiang, et al.
Publicado: (2018) -
Role
of Ligand-Driven Conformational Changes in Enzyme
Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate
Isomerase
por: Kulkarni, Yashraj S., et al.
Publicado: (2018)