Skip to Content
Merck
  • Amide compound synthesis by adenylation domain of bacillibactin synthetase.

Amide compound synthesis by adenylation domain of bacillibactin synthetase.

The Journal of antibiotics (2016-10-13)
Tomoko Abe, Yoshiteru Hashimoto, Sayaka Sugimoto, Kenta Kobayashi, Takuto Kumano, Michihiko Kobayashi
ABSTRACT

The adenylation domain of nonribosomal peptide synthetase (NRPS) is responsible for the selective substrate recognition and its activation (as an acyl-O-AMP intermediate) during ATP consumption. DhbE, a stand-alone adenylation domain, acts on an aromatic acid, 2,3-dihydroxybenzoic acid (DHB). This activation is the initial step of the synthesis of bacillibactin that is a high-affinity small-molecule iron chelator also termed siderophore. Subsequently, the activated DHB is transferred and attached covalently to a peptidyl carrier protein domain via a thioester bond. Adenylation domains belong to the superfamily of adenylate-forming enzymes including acetyl-CoA synthetase, acyl-CoA synthetase and firefly luciferase. We previously reported a novel N-acylation reaction for an acyl-CoA synthetase (AcsA) that originally catalyzes the formation of a thioester bond between an acid and CoA, yielding acyl-CoA. This novel reaction was also confirmed for acetyl-CoA synthetase and firefly luciferase, but not yet for an adenylation domain. Here, we for the first time demonstrated the synthesis of N-acyl-L-cysteine by a stand-alone adenylation domain, DhbE. When DHB and L-cysteine were used as substrates of DhbE, N-DHB-L-cysteine was formed. A V

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
3-Cyanobenzoic acid, 98%
Sigma-Aldrich
4-Cyanobenzoic acid, 99%
Sigma-Aldrich
Taurolidine, >97% (NMR), powder
Sigma-Aldrich
2,6-Difluorobenzoic acid, 98%