Structural highlights
Function
BESA_STREN Involved in the biosynthesis of terminal alkyne-containing amino acids such as L-beta-ethynylserine, that are produced as antibiotics by S.cattleya. Catalyzes the ATP-dependent ligation of L-propargylglycine to L-glutamate to form the dipeptide L-gamma-glutamyl-L-propargylglycine. Is selective for L-propargylglycine over norvaline, allylglycine and the standard proteinogenic amino acids, except L-cysteine which can be used as a substrate to a lesser extent.[1]
References
- ↑ Marchand JA, Neugebauer ME, Ing MC, Lin CI, Pelton JG, Chang MCY. Discovery of a pathway for terminal-alkyne amino acid biosynthesis. Nature. 2019 Mar;567(7748):420-424. doi: 10.1038/s41586-019-1020-y. Epub 2019 Mar, 13. PMID:30867596 doi:http://dx.doi.org/10.1038/s41586-019-1020-y
