Cargando…
Structural and Functional Analysis of the Complex between Citrate and the Zinc Peptidase Carboxypeptidase A
A high-resolution carboxypeptidase-Zn(2+)-citrate complex was studied by X-ray diffraction and enzyme kinetics for the first time. The citrate molecule acts as a competitive inhibitor of this benchmark zinc-dependent peptidase, chelating the catalytic zinc ion in the active site of the enzyme and in...
Autores principales: | Fernández, Daniel, Boix, Ester, Pallarès, Irantzu, Avilés, Francesc X., Vendrell, Josep |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
SAGE-Hindawi Access to Research
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3144702/ https://www.ncbi.nlm.nih.gov/pubmed/21804935 http://dx.doi.org/10.4061/2011/128676 |
Ejemplares similares
-
Self-assembly of human latexin into amyloid-like oligomers
por: Pallarés, Irantzu, et al.
Publicado: (2007) -
Prediction of "hot spots" of aggregation in disease-linked polypeptides
por: de Groot, Natalia Sánchez, et al.
Publicado: (2005) -
Structure–Function Analysis of the Short Splicing Variant Carboxypeptidase Encoded by Drosophila melanogaster silver
por: Tanco, Sebastián, et al.
Publicado: (2010) -
Substrate specificity of human metallocarboxypeptidase D: Comparison of the two active carboxypeptidase domains
por: Garcia-Pardo, Javier, et al.
Publicado: (2017) -
CARBOXYPEPTIDASE : III. THE ESTIMATION OF CARBOXYPEPTIDASE AND PRO-CARBOXYPEPTIDASE
por: Anson, M. L.
Publicado: (1937)