Journal
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
Volume 33, Issue 1, Pages -Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/14756366.2017.1422250
Keywords
Carbonic anhydrase; metalloenzymes; pathogens; activators; Mycobacterium tuberculosis
Funding
- Distinguished Scientist Fellowship Programme (DSFP) of King Saud University, Saudi Arabia
- Australian Research Council [DP160102681]
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The activation of a beta-class carbonic anhydrase (CAs, EC 4.2.1.1) from Mycobacterium tuberculosis, encoded by the gene Rv3273 (mtCA 3), was investigated using a panel of natural and non-natural amino acids and amines. mtCA 3 was effectively activated by D-DOPA, L-Trp, dopamine and serotonin, with K(A)s ranging between 8.98 and 12.1 mu M. L-His and D-Tyr showed medium potency activating effects, with K(A)s in the range of 17.6-18.2 mu M, whereas other amines and amino acids were relatively ineffective activators, with K(A)s in the range of 28.9-52.2 mu M. As the physiological roles of the three mtCAs present in this pathogen are currently poorly understood and considering that inhibition of these enzymes has strong antibacterial effects, discovering molecules that modulate their enzymatic activity may lead to a better understanding of the factors related to the invasion and colonisation of the host during Mycobacterium tuberculosis infection.
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