Cited by 42Enzyme function and inhibitionEnzyme Structure and FunctionBiochemical and Molecular Research

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The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide

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Håkansson, K., Liljas, A.·1994·FEBS Letters

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It has recently been shown that aliphatic sulphonamides are good inhibitors of carbonic anhydrase (CA) provided that the pK of the sulphonamide is low. We have determined the structure of the complex between CAII and CF 3 SO 2 NH 2 by X‐ray crystallographic methods. The nitrogen of the sulphonamide is bound to the zinc ion of the enzyme in the usual manner. The other parts of the inhibitor show a different mode of binding from aromatic sulphonamides since the trifluoromethyl group is bound at the hydrophobic part of the active site instead of pointing out from the active site. It should be possible to design new inhibitors specific for the different isoenzymes, starting from the present structure.

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Authors: Håkansson, K., & Liljas, A.
Affiliations: Lund University (SE)
Corresponding author: Liljas, A.
ORCID: Liljas, A.
Venue: FEBS Letters
Publisher: Wiley
Published: 1994-08-22
Volume: 350
Issue: 2-3
Pages: 319-322
ISSN: 0014-5793 (ISSN-L)
1873-3468
DOI: 10.1016/0014-5793(94)00798-5
OpenAlex: W2020999457
Cited by: 36
References: 29
Citations by year: 2021: 3 · 2018: 1 · 2015: 1 · 2014: 2 · 2012: 2
FWCI: 1.27
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 2615 d)
Locations: FEBS Letters (publishedVersion)
PubMed (publishedVersion)
Funders: Knut och Alice Wallenbergs Stiftelse
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords: carbonic anhydrase II, enzyme-inhibitor complex, zinc binding, hydrophobic binding, active site, inhibitor design, isozymes
MeSH terms: Binding Sites, Carbonic Anhydrases, Carbonic Anhydrase Inhibitors, Chlorofluorocarbons, Methane, Humans, Models, Molecular, Sulfonamides, Crystallography, X-Ray

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The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide

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