Kinetic and anion inhibition studies of a beta-carbonic anhydrase (FbiCA 1) from the C4 plant Flaveria bidentis.

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Monti SM, De Simone G, Dathan NA, Ludwig M, Vullo D, Scozzafava A, Capasso C, Supuran CT

Kinetic and anion inhibition studies of a beta-carbonic anhydrase (FbiCA 1) from the C4 plant Flaveria bidentis.

Bioorg Med Chem Lett. 2013 Mar 15;23(6):1626-30. doi: 10.1016/j.bmcl.2013.01.087. Epub 2013 Jan 30.

PubMed ID

23414801 [ View in PubMed

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Abstract

Several beta-carbonic anhydrases (CAs, EC 4.2.1.1) are present in all land plants examined thus far. Here we report the first detailed biochemical characterization of one such isoform, FbiCA 1, from the C4 plant Flaveria bidentis, which was cloned, purified and characterized as recombinant protein. FbiCA 1 has an interesting CO2 hydrase catalytic activity (kcat of 1.2x10(5) and kcat/Km of 7.5x10(6)M(-1)xs(-1)) and was moderately inhibited by most simple/complex inorganic anions. Potent FbiCA 1 inhibitors were also detected, such as trithiocarbonate, diethyldithiocarbamate, sulfamide, sulfamic acid, phenylboronic acid and phenylarsonic acid (KIs in the range of 4-60muM). Such inhibitors may be used as tools to better understand the role of various beta-CA isoforms in photosynthesis.

DrugBank Data that Cites this Article

Binding Properties

Drug	Target	Property	Measurement	pH	Temperature (°C)
Acetazolamide	Carbonic anhydrase 1	Ki (nM)	250	N/A	N/A	Details
Acetazolamide	Carbonic anhydrase 2	Ki (nM)	12	N/A	N/A	Details