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Cloning and Characterization of Adenylyl Cyclase from Mycobacterium Tuberculosis H37Rv Reveals its Homology to the Eukaryotic Enzyme

Published

Author(s)

M A. Kamireddi, K. Dhanireddi, A M. Davis, Prasad T. Reddy

Abstract

The deduced amino acid sequence (443 aa) encoded by the adenylyl cyclase gene from the human pathogen Mycobaterium tuberculosis H37Rv (Mtb AC) is hypothesized to contain a single hydrophobic domain of six transmembrane helices in the amino terminal half of the protein. Mutagenesis of all the eight arginine residues in the amino terminal cytoplasmic tail (48 aa) abolished AC activity. It is proposed that the formation of the catalytic site in Mtb AC requires an interaction between the cytoplasmic tail and the carboxyl terminal cytoplasmic domain which has extensive homology with the catalytic core of eukaryotic adenylyl cyclases. The physiological significance of the activation of Mtb AC by manganese is discussed in view of the presence of manganese transproter protein in mycobacteria and macrophages.
Citation
Science Journal

Keywords

Adenylyl cyclase, cyclic AMP, M. tuberclosis, pathogens

Citation

Kamireddi, M. , Dhanireddi, K. , Davis, A. and Reddy, P. (2008), Cloning and Characterization of Adenylyl Cyclase from Mycobacterium Tuberculosis H37Rv Reveals its Homology to the Eukaryotic Enzyme, Science Journal (Accessed February 29, 2024)
Created October 16, 2008