Part:BBa_K2401002
2,3-dihydroxybenzoate-AMP ligase
2,3-dihydroxybenzoate-AMP ligase, this protein activates the core substrate of the pyochelin and yersiniabactin synthesis, salicylate. It activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate (ATP-PPi exchange). Enzymatic studies on the purified enzyme, 2,3DHB-AMP ligase of Escherichia coli, show that 2,3DHB efficiently supports the ATP-PPi exchange while other analogues can replace 2,3DHB.
It’s an adenylation component of non-ribosomal peptide synthases (NRPSs) and therefore involved in the biosynthesis of siderophores. It is thought to activate 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate (ATP-PPi exchange), which then activates Salicylat, the core substrate of the pyochelin and yersiniabactin synthesis, by ligation of AMP and release of pyrophosphate (ATP-PPi-exchange).
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 430
Illegal SapI site found at 456
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