Structural highlights
Function
[AMBB_PSEAE] Involved in the biosynthesis of the antimetabolite L-2-amino-4-methoxy-trans-3-butenoic acid (AMB), a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes (PubMed:20543073, PubMed:25814981). Adenylates L-alanine and loads it onto its peptidyl carrier domain via a thioester linkage to the phosphopanthetheine moiety. In addition, loads activated L-Ala in trans onto the second carrier domain of AmbE (PubMed:25814981). Can also activate L-Ser, Gly and D-Ala, albeit to a lower extent (PubMed:25814981). The condensation domain of AmbB probably condenses the activated L-Ala and the L-Glu loaded on AmbE to form a L-Glu-L-Ala dipeptide at the first carrier domain of AmbE (PubMed:25814981).[1] [2]
References
- ↑ Lee X, Fox A, Sufrin J, Henry H, Majcherczyk P, Haas D, Reimmann C. Identification of the biosynthetic gene cluster for the Pseudomonas aeruginosa antimetabolite L-2-amino-4-methoxy-trans-3-butenoic acid. J Bacteriol. 2010 Aug;192(16):4251-5. doi: 10.1128/JB.00492-10. Epub 2010 Jun 11. PMID:20543073 doi:http://dx.doi.org/10.1128/JB.00492-10
- ↑ Rojas Murcia N, Lee X, Waridel P, Maspoli A, Imker HJ, Chai T, Walsh CT, Reimmann C. The Pseudomonas aeruginosa antimetabolite L -2-amino-4-methoxy-trans-3-butenoic acid (AMB) is made from glutamate and two alanine residues via a thiotemplate-linked tripeptide precursor. Front Microbiol. 2015 Mar 12;6:170. doi: 10.3389/fmicb.2015.00170. eCollection, 2015. PMID:25814981 doi:http://dx.doi.org/10.3389/fmicb.2015.00170
