Study of zinc protein ligands in a halophilic enzyme

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Title: Study of zinc protein ligands in a halophilic enzyme
Authors: Esclapez Espliego, Julia María | Baker, Patrick J. | Rice, David W. | Pire, Carmen | Ferrer, Juan | Bonete, María-José
Research Group/s: Biotecnología de Extremófilos (BIOTECEXTREM)
Center, Department or Service: Universidad de Alicante. Departamento de Agroquímica y Bioquímica
Keywords: Archaea | Catalytic zinc | Glucose dehydrogenase | Structural analysis
Knowledge Area: Bioquímica y Biología Molecular
Issue Date: 2014
Publisher: Research Trends
Citation: Current Topics in Peptide & Protein Research. 2014, 15: 91-98
Abstract: Glucose dehydrogenase (EC 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.
ISSN: 0972-4524
Language: eng
Type: info:eu-repo/semantics/article
Rights: © 2014 Research Trends
Peer Review: si
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Appears in Collections:INV - BIOTECEXTREM - Artículos de Revistas
INV - AppBiochem - Artículos de Revistas

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