AMB antimetabolite synthase AmbE

UniProtKB accession:  Q9I1H3

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UniProtKB description:  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-glutamate and loads it onto its first peptidyl carrier domain via a thioester linkage to the phosphopanthetheine moiety (PubMed:25814981). The second peptidyl carrier domain is loaded with a L-alanine activated by AmbB (PubMed:25814981). After formation by AmbB of the L-Glu-L-Ala dipeptide at the first carrier domain of AmbE, the condensation domain of AmbE probably condenses this dipeptide with the L-Ala residue attached at the second carrier domain of AmbE to give the L-Ala-L-Glu-L-Ala tripeptide. The central amino acid, L-Glu, would then undergo a series of modifications to be converted into AMB while the two flanking L-Ala residues remain in place (PubMed:25814981). Finally, the L-Ala-AMB-L-Ala tripeptide is probably released by thioester cleavage via the thioester domain of AmbE (PubMed:25814981).