Poster's note : Relevant to DAC. Received much media coverage.  EG
Science Daily at
http://www.sciencedaily.com/releases/2015/10/151022141716.htm,

http://scripts.iucr.org/cgi-bin/paper?S1399004715012183

Acta Cryst. (2015). D71, 1745-1756
doi:10.1107/S1399004715012183
BUY ARTICLE

Structural and biophysical characterization of the -carbonic anhydrase
from the gammaproteobacteriumThiomicrospira crunogena XCL-2: insights
into engineering thermostable enzymes for CO2 sequestration

N. A. Díaz-Torres, B. P. Mahon, C. D. Boone, M. A. Pinard, C. Tu, R.
Ng, M. Agbandje-McKenna, D. Silverman, K. Scott and R. McKenna
Biocatalytic CO2 sequestration to reduce greenhouse-gas emissions from
industrial processes is an active area of research. Carbonic
anhydrases (CAs) are attractive enzymes for this process. However, the
most active CAs display limited thermal and pH stability, making them
less than ideal. As a result, there is an ongoing effort to engineer
and/or find a thermostable CA to fulfill these needs. Here, the
kinetic and thermal characterization is presented of an -CA recently
discovered in the mesophilic hydrothermal vent-isolate extremophile
Thiomicrospira crunogena XCL-2 (TcruCA), which has a significantly
higher thermostability compared with human CA II (melting temperature
of 71.9°C versus 59.5°C, respectively) but with a tenfold decrease in
the catalytic efficiency. The X-ray crystallographic structure of the
dimeric TcruCA shows that it has a highly conserved yet compact
structure compared with other -CAs. In addition, TcruCA contains an
intramolecular disulfide bond that stabilizes the enzyme. These
features are thought to contribute significantly to the
thermostability and pH stability of the enzyme and may be exploited to
engineer -CAs for applications in industrial CO2 sequestration.
Keywords: Thiomicrospira crunogena XCL-2; -carbonic anhydrase; protein
thermostability; biocatalyst; extremophile; CO2 sequestration.

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