| Literature DB >> 18993072 |
Semra Isik1, Feray Kockar, Oktay Arslan, Ozen Ozensoy Guler, Alessio Innocenti, Claudiu T Supuran.
Abstract
The protein encoded by the Nce103 gene of Saccharomyces cerevisiae, a beta-carbonic anhydrase (CA, EC 4.2.1.1) designated as scCA, has been cloned, purified, characterized kinetically, and investigated for its inhibition with a series simple, inorganic anions such as halogenides, pseudohalogenides, bicarbonate, carbonate, nitrate, nitrite, hydrogen sulfide, bisulfite, perchlorate, sulfate, and some of its isosteric species. The enzyme showed high CO(2) hydrase activity, with a k(cat) of 9.4x10(5) s(-1) and k(cat)/K(m) of 9.8x10(7) M(-1) s(-1). scCA was weakly inhibited by metal poisons (cyanide, azide, cyanate, thiocyanate, K(I)s of 16.8-55.6 mM) and strongly inhibited by bromide, iodide, and sulfamide (K(I)s of 8.7-10.8 microM). The other investigated anions showed inhibition constants in the low millimolar range.Entities:
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Year: 2008 PMID: 18993072 DOI: 10.1016/j.bmcl.2008.10.100
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN: 0960-894X Impact factor: 2.823