Anthrax edema factor: Difference between revisions
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== Function == | == Function == | ||
'''Anthrax edema factor''' (EF) or '''calmodulin-sensitive adenylate cyclase''' is an enzyme which is part of the ''Bacillus anthracis'' anthrax toxin. The full anthrax toxin is composed of | '''Anthrax edema factor''' (EF) or '''calmodulin-sensitive adenylate cyclase''' is an enzyme which is part of the ''Bacillus anthracis'' anthrax toxin. The full anthrax toxin is composed of -<BR /> | ||
*A cell-binding protein [[Anthrax protective antigen]])<BR /> | |||
*[[Anthrax Lethal Factor]]<BR /> | |||
*and anthrax edema factor.<br /> | |||
The EF is a calcium- and calmodulin-dependent adenylate cyclase. The binding of calmodulin to EF changes it from its non-active form to the active one.<ref>PMID:15680766</ref> See also [[Toxins]]. | |||
== Disease == | == Disease == | ||
Revision as of 12:40, 8 January 2020
FunctionAnthrax edema factor (EF) or calmodulin-sensitive adenylate cyclase is an enzyme which is part of the Bacillus anthracis anthrax toxin. The full anthrax toxin is composed of -
The EF is a calcium- and calmodulin-dependent adenylate cyclase. The binding of calmodulin to EF changes it from its non-active form to the active one.[1] See also Toxins. DiseaseThe anthrax disease is caused by the invasion of cells by the bacteria followed by increasing the cellular level of cAMP thus upsetting water homeostasis and causing disruption of signaling pathways. Structural highlights3D structures of anthrax edema factorAnthrax edema factor 3D structures
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ReferencesReferences
- ↑ Abrami L, Reig N, van der Goot FG. Anthrax toxin: the long and winding road that leads to the kill. Trends Microbiol. 2005 Feb;13(2):72-8. PMID:15680766 doi:http://dx.doi.org/10.1016/j.tim.2004.12.004
- ↑ Shen Y, Zhukovskaya NL, Zimmer MI, Soelaiman S, Bergson P, Wang CR, Gibbs CS, Tang WJ. Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection. Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):3242-7. Epub 2004 Feb 20. PMID:14978283 doi:10.1073/pnas.0306552101