Back to Search
Start Over
Cloning, characterization and anion inhibition studies of a γ-carbonic anhydrase from the Antarctic cyanobacterium Nostoc commune.
- Source :
-
Bioorganic & medicinal chemistry letters [Bioorg Med Chem Lett] 2015 Nov 01; Vol. 25 (21), pp. 4970-4975. Date of Electronic Publication: 2015 Mar 11. - Publication Year :
- 2015
-
Abstract
- We report the cloning and catalytic activity of a γ-carbonic anhydrase (CA, EC 4.2.1.1) isolated from the Antarctic cyanobacterium Nostoc commune, NcoCA. The enzyme has a significant catalytic activity for the physiologic reaction, CO2 hydration to bicarbonate and protons, with a k(cat) of 9.5×10(5) s(-1) and a k(cat)/K(m) of 8.3×10(7) M(-1) × s(-1), being the most catalytically efficient γ-CA investigated so far. An anion inhibition study of NcoCA with inorganic/organic anions is also reported here. Fluoride, sulfate, perchlorate and tetrafluoroborate did not inhibit appreciably NcoCA, whereas the other halides, pseudohalides, bicarbonate, nitrate, nitrite and many complex inorganic anions showed inhibition in the millimolar range. The best NcoCA inhibitors detected so far were diethyldithiocarbamate (K(I) of 0.80 mM) as well as sulfamide, sulfamate, phenylboronic acid and phenylarsonic acid (K(I)s in the range of 70-90 μM). Since γ-CAs are present in carboxysomes, being involved in photosynthesis, this study may be relevant for a better understanding of such processes in some Antarctic organisms.<br /> (Copyright © 2015 Elsevier Ltd. All rights reserved.)
- Subjects :
- Anions chemistry
Anions isolation & purification
Anions pharmacology
Biocatalysis drug effects
Carbonic Anhydrase Inhibitors chemistry
Carbonic Anhydrase Inhibitors isolation & purification
Cloning, Molecular
Dose-Response Relationship, Drug
Molecular Structure
Structure-Activity Relationship
Carbonic Anhydrase Inhibitors pharmacology
Carbonic Anhydrases metabolism
Nostoc commune enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1464-3405
- Volume :
- 25
- Issue :
- 21
- Database :
- MEDLINE
- Journal :
- Bioorganic & medicinal chemistry letters
- Publication Type :
- Academic Journal
- Accession number :
- 25804721
- Full Text :
- https://doi.org/10.1016/j.bmcl.2015.03.010