Literature

Abstract

Sulthiame, a clinically used antiepileptic, was investigated for its interaction with 12 catalytically active mammalian carbonic anhydrase (CA, EC 4.2.1.1) isoforms. The drug is a potent inhibitor of CA II, VII, IX, and XII (K(I)s of 6-56 nM), and a medium potency inhibitor against CA IV, VA, VB, and VI (K(I)s of 81-134 nM). The high resolution crystal structure of the hCA II-sulthiame adduct revealed a large number of favorable interactions between the drug and the enzyme which explain its strong low nanomolar affinity for this isoform and may also be exploited for the design of effective inhibitors incorporating sultam moieties.

DOI： 10.1016/j.bmcl.2007.06.044

Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: Kinetic and X-ray crystallographic studies

Bioorganic & Medicinal Chemistry Letters 2007.0

Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide with 12 mammalian isoforms: Kinetic and X-ray crystallographic studies

Bioorganic & Medicinal Chemistry Letters 2008.0

Carbonic Anhydrase Inhibitors: Clash with Ala65 as a Means for Designing Inhibitors with Low Affinity for the Ubiquitous Isozyme II, Exemplified by the Crystal Structure of the Topiramate Sulfamide Analogue

Journal of Medicinal Chemistry 2006.0

Sultam based Carbonic Anhydrase VII inhibitors for the management of neuropathic pain

European Journal of Medicinal Chemistry 2022.0

Carbonic anhydrase inhibitors: SAR and X-ray crystallographic study for the interaction of sugar sulfamates/sulfamides with isozymes I, II and IV

Bioorganic & Medicinal Chemistry Letters 2003.0

Carbonic anhydrase inhibitors: X-ray crystallographic structure of the adduct of human isozyme II with the antipsychotic drug sulpiride