Structure and Catalysis by Carbonic Anhydrase II: Role of Active-Site Tryptophan 5

Publication year: 2011 Source: Archives of Biochemistry and Biophysics, Available online 4 October 2011 Rose Mikulski, John F. Domsic, George Ling, Chingkuang Tu, Arthur H. Robbins, … The tryptophan residue Trp5, highly conserved in the α class of carbonic anhydrases including human carbonic anhydrase II (HCA II), is positioned at the entrance of the active site cavity and forms a π-stacking interaction with the imidazole ring of the proton shuttle His64 in its outward orientation

Publication year: 2011 Source: Archives of Biochemistry and Biophysics, Available online 4 October 2011 Rose Mikulski, John F. Domsic, George Ling, Chingkuang Tu, Arthur H. Robbins, … The tryptophan residue Trp5, highly conserved in the α class of carbonic anhydrases including human carbonic anhydrase II (HCA II), is positioned at the entrance of the active site cavity and forms a π-stacking interaction with the imidazole ring of the proton shuttle His64 in its outward orientation

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Structure and Catalysis by Carbonic Anhydrase II: Role of Active-Site Tryptophan 5

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