期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1804, 期 2, 页码 326-331出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2009.07.025
关键词
Carbonic anhydrase; Carbon dioxide; Sequestration of carbon dioxide
资金
- NIH [GM 25154]
The interaction between carbon dioxide (CO2) and the alpha-class carbonic anhydrase, human CA 2 (HCA2) exists for only a short period due to the rapid catalytic turnover by this enzyme. The fleeting nature of this interaction has led to difficulties in its direct analysis, with previous studies placing the CO2 in the hydrophobic pocket of HCA2's active site. A more precise location was determined via the crystal structure of CO2 trapped in both wild-type (holo) and zinc-free (apo) HCA2. This provided a detailed description of the means by which CO2 is held and orientated for optimal catalysis. This information can be extended to the beta and gamma class enzymes to help elucidate the binding mode of CO2 in these enzymes. (C) 2009 Elsevier B.V. All rights reserved.
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