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KMID : 0613820110210030473
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Journal of Life Science
2011 Volume.21 No. 3 p.473 ~ p.479
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Adenylyl Cyclases in Mycobacteria
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Jeon Han-Seung
Ko In-Jeong
Oh Jeong-Il
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Abstract
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Adenylyl cyclase (AC) catalyzes the formation of cyclic AMP (cAMP) from ATP. The cAMP produced by AC serves as a secondary messenger in a variety of signal transduction pathways, and controls various cellular functions in many organisms. ACs can be grouped into six classes based on their primary amino acid sequences. Eukaryotes and mycobacteria contain only members of class Ⅲ AC. The catalytic cyclase domains of class Ⅲ AC are active as dimers: mammalian ACs, which are composed of a single polypeptide with two catalytic cyclase domains, form the active site as a result of intramolecular dimerization of the catalytic cyclase domains. In contrast, mycobacterial ACs function as homodimers, since their polypeptides contain a single catalytic cyclase domain. Six amino acids are required for the catalytic activity of class Ⅲ AC - two aspartate residues, a lysine-aspartate pair and an arginine-asparagine pair. 16 ACs belonging to the class Ⅲ were identified in Mycobacterium tuberculosis H37Rv, and their characteristics are reviewed.
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KEYWORD
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Adenylyl cyclase, cAMP, Mycobacterium tuberculosis, secondary messenger, signal transduction pathway
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