Number of the records: 1
Acylation of lysine 983 is sufficient for toxin activity of Bordetella pertussis adenylate cyclase
- 1.0153807 - MBU-M 20010086 RIV US eng J - Journal Article
Basar, T. - Havlíček, Vladimír - Bezoušková, Silvia - Hackett, M. - Šebo, Peter
Acylation of lysine 983 is sufficient for toxin activity of Bordetella pertussis adenylate cyclase.
Journal of Biological Chemistry. Roč. 276, č. 1 (2001), s. 348-354. ISSN 0021-9258. E-ISSN 1083-351X
R&D Projects: GA ČR GA310/98/0432; GA ČR GV310/96/K102; GA AV ČR IAA5020907; GA MŠMT ME 167; GA MŠMT VS96149
Institutional research plan: CEZ:A53/98:Z5-020-9ii
Subject RIV: EE - Microbiology, Virology
Impact factor: 7.258, year: 2001
The capacity of adenylate cyclase toxin (ACT) to penetrate into target cells depends on post-translational fatty-acylation by the acyltransferase Cyac, which can palmitoylate the conserved lysines 983 and 860 of ACT.
Permanent Link: http://hdl.handle.net/11104/0051299
Number of the records: 1