1cay: Difference between revisions

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==Overview==

The molecular structures of the acetate complexes of wild-type human, carbonic anhydrase II (HCAII) and of E106Q mutant human carbonic anhydrase, II were solved with high completeness (89-91%) to 2.1 and 1.9 A, resolution, respectively. Both wild-type and mutant enzyme crystallize in, space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and, beta = 104.6 degrees. The altered active-site hydrogen-bond network caused, by the mutation results in a different binding of the inhibitor in the two, complexes. In the mutant, but not in the wild-type complex, a carboxylate, O atom is within hydrogen-bond distance of Thr199 Ogamma1. In the, wild-type enzyme ligand hydrogen bonding to this atom is normally only, found for hydrogen-bond donors. The importance of this discrimination on, catalysis by the enzyme is discussed briefly.

The molecular structures of the acetate complexes of wild-type human carbonic anhydrase II (HCAII) and of E106Q mutant human carbonic anhydrase II were solved with high completeness (89-91%) to 2.1 and 1.9 A resolution, respectively. Both wild-type and mutant enzyme crystallize in space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and beta = 104.6 degrees. The altered active-site hydrogen-bond network caused by the mutation results in a different binding of the inhibitor in the two complexes. In the mutant, but not in the wild-type complex, a carboxylate O atom is within hydrogen-bond distance of Thr199 Ogamma1. In the wild-type enzyme ligand hydrogen bonding to this atom is normally only found for hydrogen-bond donors. The importance of this discrimination on catalysis by the enzyme is discussed briefly.

==Disease==

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[[Category: lyase(oxo-acid)]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:34:50 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:14 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The molecular structures of the acetate complexes of wild-type human, carbonic anhydrase II (HCAII) and of E106Q mutant human carbonic anhydrase, II were solved with high completeness (89-91%) to 2.1 and 1.9 A, resolution, respectively. Both wild-type and mutant enzyme crystallize in, space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and, beta = 104.6 degrees. The altered active-site hydrogen-bond network caused, by the mutation results in a different binding of the inhibitor in the two, complexes. In the mutant, but not in the wild-type complex, a carboxylate, O atom is within hydrogen-bond distance of Thr199 Ogamma1. In the, wild-type enzyme ligand hydrogen bonding to this atom is normally only, found for hydrogen-bond donors. The importance of this discrimination on, catalysis by the enzyme is discussed briefly.
+The molecular structures of the acetate complexes of wild-type human carbonic anhydrase II (HCAII) and of E106Q mutant human carbonic anhydrase II were solved with high completeness (89-91%) to 2.1 and 1.9 A resolution, respectively. Both wild-type and mutant enzyme crystallize in space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and beta = 104.6 degrees. The altered active-site hydrogen-bond network caused by the mutation results in a different binding of the inhibitor in the two complexes. In the mutant, but not in the wild-type complex, a carboxylate O atom is within hydrogen-bond distance of Thr199 Ogamma1. In the wild-type enzyme ligand hydrogen bonding to this atom is normally only found for hydrogen-bond donors. The importance of this discrimination on catalysis by the enzyme is discussed briefly.
 ==Disease==
@@ Line 26: / Line 26: @@
 [[Category: lyase(oxo-acid)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:34:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:14 2008''