Zeta-carbonic anhydrases show CS

AAZ, Acetazolamide CA, Carbonic Anhydrase CAI, Carbonic Anhydrase Inhibitor CCD, Charge Coupled Device CDCA1, Cadmium-specific Carbonic Anhydrase CO2 CS2 CS2H, S. solfataricus CS2 hydrolase Cambialistic enzyme Carbonic Anhydrase DMSO, Dimethyl Sulfoxide FbiCA, Flaveria bidentis Carbonic Anhydrase HEPES, 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid IPTG, Isopropyl-β-D-1-thiogalactopyranoside MD, Molecular Dynamics Molecular dynamics NCS, Non-Crystallographic Symmetry PDB, Protein Data Bank PEG, Polyethylene glycol SDS-PAGE, Sodium Dodecyl Sulphate - PolyAcrylamide Gel Electrophoresis Tris-HCl, Tris(hydroxymethyl)aminomethane hydrochloride bCA, bovine Carbonic Anhydrase hCA, human Carbonic Anhydrase psCA3, Pseudomonas aeruginosa Carbonic Anhydrase 3

Journal

Computational and structural biotechnology journal
ISSN: 2001-0370
Titre abrégé: Comput Struct Biotechnol J
Pays: Netherlands
ID NLM: 101585369

Informations de publication

Date de publication:
2021
Historique:
received: 16 04 2021
revised: 27 05 2021
accepted: 30 05 2021
entrez: 1 7 2021
pubmed: 2 7 2021
medline: 2 7 2021
Statut: epublish

Résumé

CDCA1 is a very peculiar member of the Carbonic Anhydrase (CA) family. It has been the first enzyme to show an efficient utilization of Cd(II) ions in Nature and a unique adaptation capability to live on the surface ocean. Indeed, in this environment, which is extremely depleted in essential metal ions, CDCA1 can utilize Zn(II) or Cd(II) as catalytic metal to support the metabolic needs of fast growing diatoms. In this paper we demonstrate a further catalytic versatility of this enzyme by using a combination of X-ray crystallography, molecular dynamics simulations and enzymatic experiments. First we identified the CO

Identifiants

pubmed: 34194668
doi: 10.1016/j.csbj.2021.05.057
pii: S2001-0370(21)00246-4
pmc: PMC8217695
doi:

Types de publication

Journal Article

Langues

eng

Pagination

3427-3436

Informations de copyright

© 2021 The Authors. Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology.

Déclaration de conflit d'intérêts

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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Auteurs

Vincenzo Alterio (V)

Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy.

Emma Langella (E)

Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy.

Martina Buonanno (M)

Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy.

Davide Esposito (D)

Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy.

Alessio Nocentini (A)

NEUROFARBA Department, Pharmaceutical and Nutraceutical Section, University of Firenze, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Italy.

Emanuela Berrino (E)

NEUROFARBA Department, Pharmaceutical and Nutraceutical Section, University of Firenze, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Italy.

Silvia Bua (S)

NEUROFARBA Department, Pharmaceutical and Nutraceutical Section, University of Firenze, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Italy.

Maurizio Polentarutti (M)

Elettra - Sincrotrone Trieste, s.s. 14 Km 163.5 in Area Science Park, Basovizza (Trieste) 34149, Trieste, Italy.

Claudiu T Supuran (CT)

NEUROFARBA Department, Pharmaceutical and Nutraceutical Section, University of Firenze, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Italy.

Simona Maria Monti (SM)

Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy.

Giuseppina De Simone (G)

Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy.

Classifications MeSH