Now showing items 1-5 of 5
Saccharomyces cerevisiae beta-carbonic anhydrase: ınhibition and activation studies
(Bentham Science Publ Ltd, 2010)
The beta-carbonic anhydrase from Saccharomyces cerevisiae (CA, EC 220.127.116.11), scCA, which is encoded by the Nce103 gene, is an effective catalyst for CO2 hydration to bicarbonate and protons, with a k(cat) of 9.4 x 10(5) ...
Mutation of active site residues Asn67 to Ile, Gln92 to Val and Leu204 to Ser in human carbonic anhydrase ii: influences on the catalytic activity and affinity for inhibitors
(Pergamon-Elsevier Science Ltd, 2012)
Site-directed mutagenesis has been used to change three amino acid residues involved in the binding of inhibitors (Asn67Ile; Gln92Val and Leu204Ser) within the active site of human carbonic anhydrase (CA, EC 18.104.22.168) II ...
Carbonic anhydrase inhibitors: Inhibition of the β-class enzyme from the yeast Saccharomyces cerevisiae with sulfonamides and sulfamates
(Pergamon-Elsevier Science Ltd, 2009)
The protein encoded by the Nce103 gene of Saccharomyces cerevisiae, a beta-carbonic anhydrase ( CA, EC 22.214.171.124) designated as scCA, has been cloned, purified, characterized kinetically and investigated for its inhibition ...
Sulfonamide inhibition study of the beta-class carbonic anhydrase from the caries producing pathogen streptococcus mutans
(Pergamon-Elsevier Science Ltd, 2015)
Streptococcus mutans, the oral pathogenic bacterium provoking dental caries formation, encodes for a beta-class carbonic anhydrase (CA, EC 126.96.36.199), SmuCA. This enzyme was cloned, characterized and investigated for its ...
Mutation of phe91 to asn in human carbonic anhydrase ı unexpectedly enhanced both catalytic activity and affinity for sulfonamide inhibitors
(Pergamon-Elsevier Science Ltd, 2010)
Site-directed mutagenesis has been used to change one amino acid residue considered non essential (Phe91Asn) to catalysis in carbonic anhydrase (CA, EC 188.8.131.52) isozyme I (hCA I), but which is near the substrate binding ...