Structural highlights
Function
[PYLB_METBF] Catalyzes the isomerization of L-lysine to (2R,3R)-3-methylornithine via a radical-based mechanism, a step in the biosynthesis pathway of pyrrolysine.[1] [2]
Publication Abstract from PubMed
Made by the barrel load: The biosynthetic pathway of the recently discovered 22nd amino acid, pyrrolysine, starts with an isomerization of lysine to methylornithine, catalyzed by PylB. The X-ray crystal structure of PylB is determined and shows it has a TIM barrel fold. The sealed central cavity contains a [4Fe-4S] cluster, S-adenosylmethionine (SAM), and methylornithine, whose 2R,3R configuration could be confirmed. The data suggest a fragmentation-recombination mechanism via a glycyl radical intermediate.
Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis.,Quitterer F, List A, Eisenreich W, Bacher A, Groll M Angew Chem Int Ed Engl. 2011 Nov 16. doi: 10.1002/anie.201106765. PMID:22095926[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gaston MA, Zhang L, Green-Church KB, Krzycki JA. The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. Nature. 2011 Mar 31;471(7340):647-50. doi: 10.1038/nature09918. PMID:21455182 doi:http://dx.doi.org/10.1038/nature09918
- ↑ Quitterer F, List A, Eisenreich W, Bacher A, Groll M. Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis. Angew Chem Int Ed Engl. 2011 Nov 16. doi: 10.1002/anie.201106765. PMID:22095926 doi:10.1002/anie.201106765
- ↑ Quitterer F, List A, Eisenreich W, Bacher A, Groll M. Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis. Angew Chem Int Ed Engl. 2011 Nov 16. doi: 10.1002/anie.201106765. PMID:22095926 doi:10.1002/anie.201106765
