Study of zinc protein ligands in a halophilic enzyme
Empreu sempre aquest identificador per citar o enllaçar aquest ítem
http://hdl.handle.net/10045/46977
Títol: | Study of zinc protein ligands in a halophilic enzyme |
---|---|
Autors: | Esclapez, Julia | Baker, Patrick J. | Rice, David W. | Pire, Carmen | Ferrer, Juan | Bonete, María-José |
Grups d'investigació o GITE: | Biotecnología de Extremófilos (BIOTECEXTREM) |
Centre, Departament o Servei: | Universidad de Alicante. Departamento de Agroquímica y Bioquímica |
Paraules clau: | Archaea | Catalytic zinc | Glucose dehydrogenase | Structural analysis |
Àrees de coneixement: | Bioquímica y Biología Molecular |
Data de publicació: | 2014 |
Editor: | Research Trends |
Citació bibliogràfica: | Current Topics in Peptide & Protein Research. 2014, 15: 91-98 |
Resum: | Glucose dehydrogenase (EC 1.1.1.47) from the halophilic Archaeon Haloferax mediterranei belongs to the medium-chain alcohol dehydrogenase superfamily and requires a zinc ion for catalysis. The zinc ion is coordinated by a histidine, a water molecule and two other ligands from the protein or the substrate, which vary during the catalytic cycle of the enzyme. In many enzymes of this superfamily one of the zinc ligands is commonly cysteine, which is replaced by an aspartate residue at position 38 in the halophilic enzyme. This change has been only observed in glucose dehydrogenases from extremely halophilic microorganisms belonging to the Archaea Domain. This paper describes biochemical studies and structural comparisons to analyze the role of sequence differences between thermophilic and halophilic glucose dehydrogenases which contain a zinc ion within the protein surrounded by three ligands. Whilst the catalytic activity of the D38C GlcDH mutant is reduced, its thermal stability is enhanced, consistent with the greater structural similarity between this mutant and the homologous thermophilic enzyme from Thermoplasma acidophilum. |
URI: | http://hdl.handle.net/10045/46977 |
ISSN: | 0972-4524 |
Idioma: | eng |
Tipus: | info:eu-repo/semantics/article |
Drets: | © 2014 Research Trends |
Revisió científica: | si |
Versió de l'editor: | http://www.researchtrends.net/tia/abstract.asp?in=0&vn=15&tid=26&aid=5670&pub=2014&type=3 |
Apareix a la col·lecció: | INV - BIOTECEXTREM - Artículos de Revistas INV - AppBiochem - Artículos de Revistas |
Arxius per aquest ítem:
Arxiu | Descripció | Tamany | Format | |
---|---|---|---|---|
2014_Esclapez_etal_CTP&PR.pdf | 159,38 kB | Adobe PDF | Obrir Vista prèvia | |
Tots els documents dipositats a RUA estan protegits per drets d'autors. Alguns drets reservats.