YcaO

YcaO is a protein found in bacteria which is involved in the synthesis of thiazole/oxazole modified microcin antibiotics, such as bottromycin. YcaO performs ATP dependent cylodehydration to form the oxazole and thiazole moieties of the microcin.[2][3][4]

YcaO-like family
Structure of the heterocyclase TruD. A YcaO-like protein from Prochloron sp. 06037A PDB entry 4bs9[1]
Identifiers
SymbolYcaO
PfamPF02624
InterProIPR003776

References

  1. Koehnke, J.; Bent, A. F.; Zollman, D.; Smith, K.; Houssen, W. E.; Zhu, X.; Mann, G.; Lebl, T.; Scharff, R.; Shirran, S.; Botting, C. H.; Jaspars, M.; Schwarz-Linek, U.; Naismith, J. H. (2013). "The Cyanobactin Heterocyclase Enzyme: A Processive Adenylase That Operates with a Defined Order of Reaction". Angewandte Chemie International Edition. 52 (52): 13991–13996. doi:10.1002/anie.201306302. PMC 3995012. PMID 24214017.
  2. Dunbar, K. L.; Melby, J. O.; Mitchell, D. A. (2012). "YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations". Nature Chemical Biology. 8 (6): 569–575. doi:10.1038/nchembio.944. PMC 3428213. PMID 22522320.
  3. Dunbar KL, Chekan JR, Cox CL, Burkhart BJ, Nair SK, Mitchell DA (2014). "Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis". Nature Chemical Biology. 10 (10): 823–9. doi:10.1038/nchembio.1608. PMC 4167974. PMID 25129028.
  4. Koehnke J, Mann G, Bent AF, Ludewig H, Shirran S, Botting C, Lebl T, Houssen WE, Jaspars M, Naismith JH (2015). "Structural analysis of leader peptide binding enables leader-free cyanobactin processing". Nature Chemical Biology. 11: 558–63. doi:10.1038/nchembio.1841. PMC 4512242. PMID 26098679.


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