Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense
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Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense (385 views)

De Simone G, Monti SM, Alterio V, Buonanno M, De Luca V, Rossi M, Carginale V, Supuran CT, Capasso C, Di Fiore A

Bioorg Med Chem Lett (ISSN: 0960-894x), 2015 May 1; 25(9): 2002-2006.

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Paper type: Journal Article,

Impact factor: 2.486, 5-year impact factor: 2.303

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84925690260&partnerID=40&md5=1c09ed44997e4aaa2a21701dc8ffbad8

Keywords: Bacterial Carbonic Anhydrase, Proton Transfer Mechanism, Thermoactive Enzyme, Thermostable Enzyme,

Affiliations:
*** IBB - CNR ***

Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy
Seconda Università di Napoli (SUN), 81100 Caserta, Italy
Istituto di Bioscienze e Biorisorse-CNR, Via P. Castellino 111, 80131 Napoli, Italy
Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy
NEUROFARBA Department, Sezione di Scienze Farmaceutiche, Via Ugo Schiff 6, 50019 Sesto Fiorentino, Florence, Italy


References:
Not available.
Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense

Two thermostable α-carbonic anhydrases (α-CAs) isolated from thermophilic Sulfurihydrogenibium spp.; namely SspCA (from S. yellowstonensis) and SazCA (from S. azorense), were shown in a previous work to possess interesting complementary properties. SspCA was shown to have an exceptional thermal stability, whereas SazCA demonstrated to be the most active α-CA known to date for the CO2 hydration reaction. Here we report the crystallographic structure of SazCA and the identification of the structural features responsible for its high catalytic activity, by comparing it with SspCA structure. These data are of relevance for the design of engineered proteins showing higher stability and catalytic activity than other α-CAs known to date. © 2015 Elsevier Ltd.
Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense

▼    Structural characterization of proteins and enzymes isolated from organisms living under unusual conditions
Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense

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Di Fiore A, Alterio V, Monti SM, De Simone G, D’Ambrosio K
* Thermostable carbonic anhydrases in biotechnological applications (595 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2015; 16(7): 15456-15480.
Impact Factor: 3.257
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1 Records (1 excluding Abstracts).
Total impact factor: 3.257 (3.257 excluding Abstracts).
Total 5 year impact factor: 3.213 (3.213 excluding Abstracts).

Last modified by Giuseppina De Simone on Sunday 12 July 2020, 13:14:49
385 views. Last view on Monday 07 October 2024, 1:37:41