在碳酸酐酶 II 的活性部位观察到选择性疏水口袋结合，可容纳不同的 4-取代脲基苯磺酰胺类化合物，并与抑制剂的效力相关。
Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency.
机构信息
Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Box 100245, Gainesville, Florida 32610, USA.
出版信息
Chem Commun (Camb). 2010 Nov 28;46(44):8371-3. doi: 10.1039/c0cc02707c. Epub 2010 Oct 5.
PMID:20922253
Abstract
4-Substituted-ureido benzenesulfonamides showing inhibitory activity against carbonic anhydrase (CA, EC 4.2.1.1) II between 3.3-226 nM were crystallized in complex with the enzyme. Hydrophobic interactions between the scaffold of the inhibitors in different hydrophobic pockets of the enzyme were observed, explaining the diverse inhibitory range of these derivatives.
摘要
4-取代脲基苯磺酰胺类化合物对碳酸酐酶（CA，EC 4.2.1.1）表现出 3.3-226 nM 的抑制活性，与酶形成复合物结晶。抑制剂骨架与酶中不同疏水口袋之间的疏水相互作用被观察到，解释了这些衍生物具有不同的抑制范围。
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