Article ID Journal Published Year Pages File Type
1925795 Archives of Biochemistry and Biophysics 2011 7 Pages PDF
Abstract
► Replacing Tyr7 in the active site of human carbonic anhydrase II enhanced proton transfer in catalysis. ► Replacement of Try7 caused reduced thermal stability. ► Replacement of Tyr7 with Ile caused a conformational change at the amino terminus. ► Results demonstrate a role for Tyr7 in folding and stability for carbonic anhydrases in the α class.
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Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
Authors
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