scholarly journals Stabilization of anionic and neutral forms of a fluorophoric ligand at the active site of human carbonic anhydrase I

2010 ◽  
Vol 1804 (10) ◽  
pp. 1965-1973
Author(s):  
Sumathra Manokaran ◽  
Jayati Banerjee ◽  
Sanku Mallik ◽  
D.K. Srivastava
Keyword(s):  
Carbonic Anhydrase ◽  
Active Site ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase

Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I

1994 ◽  
Vol 4 (4) ◽  
pp. 294-296 ◽  
Author(s):  
W. Richard Chegwidden ◽  
Lynn E. Wagner ◽  
Patrick J. Venta ◽  
Nils C. H. Bergenhem ◽  
Ya-Shiou L. Yu ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Active Site ◽  
Ester Hydrolysis ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase

scholarly journals Synthesis and Human Carbonic Anhydrase I, II, IX, and XII Inhibition Studies of Sulphonamides Incorporating Mono-, Bi- and Tricyclic Imide Moieties

2021 ◽  
Vol 14 (7) ◽  
pp. 693
Author(s):  
Kalyan K. Sethi ◽  
KM Abha Mishra ◽  
Saurabh M. Verma ◽  
Daniela Vullo ◽  
Fabrizio Carta ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Carbonic Anhydrase ◽  
Docking Studies ◽  
Carbonic Anhydrases ◽  
Molecular Docking Studies ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase ◽  
Inhibition Studies

New derivatives were synthesised by reaction of amino-containing aromatic sulphonamides with mono-, bi-, and tricyclic anhydrides. These sulphonamides were investigated as human carbonic anhydrases (hCAs, EC 4.2.1.1) I, II, IX, and XII inhibitors. hCA I was inhibited with inhibition constants (Kis) ranging from 49 to >10,000 nM. The physiologically dominant hCA II was significantly inhibited by most of the sulphonamide with the Kis ranging between 2.4 and 4515 nM. hCA IX and hCA XII were inhibited by these sulphonamides in the range of 9.7 to 7766 nM and 14 to 316 nM, respectively. The structure–activity relationships (SAR) are rationalised with the help of molecular docking studies.

Crystal analysis of aromatic sulfonamide binding to native and (Zn)2 adduct of human carbonic anhydrase I Michigan 1

2002 ◽  
Vol 339 ◽  
pp. 135-144 ◽  
Author(s):  
Marta Ferraroni ◽  
Fabrizio Briganti ◽  
W.Richard Chegwidden ◽  
Claudiu T. Supuran ◽  
Andrea Scozzafava
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase ◽  
Aromatic Sulfonamide
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