Structural highlights
Function
[SKFB_BACSU] Catalyzes the formation of the thioether bond required for production of the sporulation killing factor (SKF) from SkfA (PubMed:12817086). Forms the cysteine-methionine thioether bond found in SKF; the acceptor amino acid can be hydrophobic, aromatic or a small hydrophilic amino acid but not a larger hydrophilic amino acid, i.e. Met=Ala, Phe, Leu, Tyr>Asn, Ser>>Gln, Glu, Lys (PubMed:23282011). The relative position of Cys and Met in the substrate cannot be inverted, in vitro the thioether bond cannot be made in the absence of the SkfA propeptide, suggesting this is the first reaction in SKF maturation (PubMed:23282011). In vitro, in the absence of a second substrate, cleaves S-adenosyl-L-methionine into Met and 5'-dA (PubMed:23282011).[1] [2]
References
- ↑ Gonzalez-Pastor JE, Hobbs EC, Losick R. Cannibalism by sporulating bacteria. Science. 2003 Jul 25;301(5632):510-3. Epub 2003 Jun 19. PMID:12817086 doi:http://dx.doi.org/10.1126/science.1086462
- ↑ Fluhe L, Burghaus O, Wieckowski BM, Giessen TW, Linne U, Marahiel MA. Two [4Fe-4S] clusters containing radical SAM enzyme SkfB catalyze thioether bond formation during the maturation of the sporulation killing factor. J Am Chem Soc. 2013 Jan 23;135(3):959-62. doi: 10.1021/ja310542g. Epub 2013 Jan, 9. PMID:23282011 doi:http://dx.doi.org/10.1021/ja310542g
