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IBBR publication #1840

Burkholderia pseudomallei γ-carbonic anhydrase is strongly activated by amino acids and amines

Vullo D, Del Prete S, Osman SM, Alothman Z, Capasso C, Donald WA, Supuran CT

Bioorganic and Medicinal Chemistry Letters 27 (1): 77-80. (2017)
doi: 10.1016/j.bmcl.2016.11.027

Activation of the c-class carbonic anhydrase (CAs, EC 4.2.1.1) from the pathogenic bacterium Burkholderia pseudomallei (BpscCA) with a series of natural and non-natural amino acids and aromatic/heterocyclic amines has been investigated. The best BpscCA activators were D-His, L-DOPA, D-Trp, 4-amino-L-Phe, dopamine, 2-(2-aminoethyl) pyridine, 2-aminoethyl-piparazine/morpholine and L-adrenaline, which showed activation constants ranging between 9 and 86 nM. The least effective activators were L-His, L-Phe and 2-pyridyl-methylamine, with K(A)s in the range of 1.73-24.7 mu M. As little is known about the role of gamma-CAs in the lifecycle and virulence of this saprophytic bacterium, this study may shed some light on such phenomena. This is the first CA activation study of a gamma-CA from a pathogenic bacterium, the only other such study being on the enzyme discovered in the archaeon Methanosarcina thermophila, Cam. (C) 2016 Elsevier Ltd. All rights reserved.

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