| Literature DB >> 26778292 |
Viviana De Luca1, Daniela Vullo2, Sonia Del Prete3, Vincenzo Carginale1, Sameh M Osman4, Zeid AlOthman4, Claudiu T Supuran5, Clemente Capasso6.
Abstract
We have cloned, purified and characterized the γ-carbonic anhydrase (CA, EC 4.2.1.1) present in the genome of the Antarctic bacterium Colwellia psychrerythraea, which is an obligate psychrophile. The enzyme shows a significant catalytic activity for the physiologic reaction of CO2 hydration to bicarbonate and protons, with the following kinetic parameters: kcat of 6.0×10(5)s(-1) and a kcat/Km of 4.7×10(6)M(-1)×s(-1). This activity was inhibited by the sulfonamide CA inhibitor (CAI) acetazolamide, with a KI of 502nM. A range of anions was also investigated for their inhibitory action against the new enzyme CpsCA. Perchlorate, tetrafluoroborate, fluoride and bromide were not inhibitory, whereas cyanate, thiocyanate, cyanide, hydrogensulfide, carbonate and bicarbonate showed KIs in the range of 1.4-4.4mM. Diethyldithiocarbamate was a better inhibitor (KI of 0.58mM) whereas sulfamide, sulfamate, phenylboronic acid and phenylarsonic acid were the most effective inhibitors detected, with KIs ranging between 8 and 38μM. The present study may shed some more light regarding the role that γ-CAs play in the life cycle of psychrophilic bacteria as the Antarctic one investigated here.Entities:
Keywords: Anions; Antarctic carbonic anhydrase; Carbonic anhydrase; Cold adaptation; Cold-enzymes; Hydratase activity; Inhibitors; Metalloenzymes; Psychrophiles
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Year: 2016 PMID： 26778292 DOI： 10.1016/j.bmc.2016.01.005
Source DB: PubMed Journal: Bioorg Med Chem ISSN： 0968-0896 Impact factor: 3.641