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

Abstract:

: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.

journal_name

Bioorg Med Chem Lett

authors

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

doi

10.1016/j.bmcl.2015.02.068

subject

Has Abstract

pub_date

2015-05-01 00:00:00

pages

2002-6

issue

9

eissn

0960-894X

issn

1464-3405

pii

S0960-894X(15)00188-2

journal_volume

25

pub_type

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