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

被引：72
作者：
De Simone, Giuseppina [1 ]
Monti, Simona Maria [1 ]
Alterio, Vincenzo [1 ]
Buonanno, Martina [1 ,2 ]
De Luca, Viviana [3 ]
Rossi, Mose [3 ]
Carginale, Vincenzo [3 ]
Supuran, Claudiu T. [4 ,5 ]
Capasso, Clemente [3 ]
Di Fiore, Anna [1 ]
机构：
[1] Ist Biostrutture & Bioimmagini CNR, I-80134 Naples, Italy
[2] SUN, I-81100 Caserta, Italy
[3] Ist Biosci & Biorisorse CNR, I-80131 Naples, Italy
[4] Univ Florence, Lab Chim Bioinorgan, Polo Sci, I-50019 Florence, Italy
[5] NEUROFARBA Dept, Sez Sci Farmaceut, I-50019 Florence, Italy
来源：
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2015年 / 25卷 / 09期
关键词：
Bacterial carbonic anhydrase; Thermostable enzyme; Thermoactive enzyme; Proton transfer mechanism; PROTON-TRANSFER; YELLOWSTONENSE YO3AOP1; INHIBITOR ACETAZOLAMIDE; EXTRACELLULAR DOMAIN; ANION INHIBITION; CO2; CAPTURE; AMINO-ACIDS; NMR SYSTEM; CA; BINDING;
D O I：
10.1016/j.bmcl.2015.02.068
中图分类号：
R914 [药物化学];
学科分类号：
100701 ;
摘要：
Two thermostable alpha-carbonic anhydrases (alpha-CAs) isolated from thermophilic Sulfurihydrogenibium spp., namely SspCA (from S. yellowstonensis) and SazCA (from Sulfurihydrogenibium 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 alpha-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 alpha-CAs known to date. (C) 2015 Elsevier Ltd. All rights reserved.
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页码：2002 / 2006
页数：5
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