Catalytic activity of a ζ-class zinc and cadmium containing carbonic anhydrase. Compared work mechanisms

2011 ◽  
Vol 13 (8) ◽  
pp. 3468 ◽  
Author(s):  
Orazio Amata ◽  
Tiziana Marino ◽  
Nino Russo ◽  
Marirosa Toscano
Keyword(s):  
Catalytic Activity ◽  
Carbonic Anhydrase

scholarly journals Azobenzene-based inhibitors of human carbonic anhydrase II

2015 ◽  
Vol 11 ◽  
pp. 1129-1135 ◽  
Author(s):  
Leander Simon Runtsch ◽  
David Michael Barber ◽  
Peter Mayer ◽  
Michael Groll ◽  
Dirk Trauner ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Activity ◽  
Carbonic Anhydrase ◽  
Drug Class ◽  
Carbonic Anhydrase Ii ◽  
Carbonic Anhydrases ◽  
X Ray ◽  
X Ray Crystallography ◽  
Human Carbonic Anhydrase

Aryl sulfonamides are a widely used drug class for the inhibition of carbonic anhydrases. In the context of our program of photochromic pharmacophores we were interested in the exploration of azobenzene-containing sulfonamides to block the catalytic activity of human carbonic anhydrase II (hCAII). Herein, we report the synthesis and in vitro evaluation of a small library of nine photochromic sulfonamides towards hCAII. All molecules are azobenzene-4-sulfonamides, which are substituted by different functional groups in the 4´-position and were characterized by X-ray crystallography. We aimed to investigate the influence of electron-donating or electron-withdrawing substituents on the inhibitory constant K i. With the aid of an hCAII crystal structure bound to one of the synthesized azobenzenes, we found that the electronic structure does not strongly affect inhibition. Taken together, all compounds are strong blockers of hCAII with K i = 25–65 nM that are potentially photochromic and thus combine studies from chemical synthesis, crystallography and enzyme kinetics.

scholarly journals Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors

2012 ◽  
Vol 22 (4) ◽  
pp. 1560-1564 ◽  
Author(s):  
Emanuela Truppo ◽  
Claudiu T. Supuran ◽  
Annamaria Sandomenico ◽  
Daniela Vullo ◽  
Alessio Innocenti ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Carbonic Anhydrase

Highly active enzymes immobilized in large pore colloidal mesoporous silica nanoparticles

2019 ◽  
Vol 43 (4) ◽  
pp. 1671-1680 ◽  
Author(s):  
Dorothée Gößl ◽  
Helena Singer ◽  
Hsin-Yi Chiu ◽  
Alexandra Schmidt ◽  
Martina Lichtnecker ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Carbonic Anhydrase ◽  
Horseradish Peroxidase ◽  
Mesoporous Silica ◽  
Silica Nanoparticles ◽  
Mesoporous Silica Nanoparticles ◽  
Click Reactions ◽  
Highly Active ◽  
Large Pore ◽  
Colorimetric Assays

Carbonic anhydrase and horseradish peroxidase are immobilized inside the ordered material by click reactions. Colorimetric assays prove their catalytic activity.

scholarly journals Anion Inhibition Studies of the β-Class Carbonic Anhydrase CAS3 from the Filamentous Ascomycete Sordaria macrospora

Metabolites ◽  
2020 ◽  
Vol 10 (3) ◽  
pp. 93
Author(s):  
Daniela Vullo ◽  
Ronny Lehneck ◽  
William A. Donald ◽  
Stefanie Pöggeler ◽  
Claudiu T. Supuran
Keyword(s):  
Catalytic Activity ◽  
Carbonic Anhydrase ◽  
Small Molecules ◽  
Small Molecule ◽  
Hydration Reaction ◽  
High Catalytic Activity ◽  
Sordaria Macrospora ◽  
Filamentous Ascomycete ◽  
Diethyl Dithiocarbamate ◽  
Inhibition Studies

CAS3 is a newly cloned cytosolic β-class carbonic anhydrase (CA, EC 4.2.1.1) from the filamentous ascomycete Sordaria macrospora. This enzyme has a high catalytic activity for the physiological CO2 hydration reaction and herein, we report the inhibition profile of CAS3 with anions and small molecules. The most effective CAS3 anions/small molecule inhibitors were diethyl-dithiocarbamate, sulfamide, sulfamate, phenyl boronic and phenyl arsonic acids, with KIs in the range of 0.89 mM–97 µM. Anions such as iodide, the pseudohalides, bicarbonate, carbonate, nitrate, nitrite, hydrogensulfide, stannate, selenate, tellurate, tetraborate, perrhenate, perruthenate, selenocyanide and trithiocarbonate were low millimolar CAS3 inhibitors. The light halides, sulfate, hydrogensulfite, peroxydisulfate, diphosphate, divanadate, perchlorate, tetrafluoroborate, fluorosulfonate and iminodisulfonate did not significantly inhibit this enzyme. These data may be useful for developing antifungals based on CA inhibition, considering the fact that many of the inhibitors reported here may be used as lead molecules and, by incorporating the appropriate organic scaffolds, potent nanomolar inhibitors could be developed.

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