2,3-dihydroxybenzoate—serine ligase
| Enterbobactin synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.2.14 | ||||||||
| CAS no. | 37318-63-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an enterobactin synthase (2,3-dihydroxybenzoate—serine ligase, EC 6.3.2.14) is an enzyme that catalyzes the chemical reaction
- ATP + 2,3-dihydroxybenzoate + L-serine products of ATP breakdown + N-(2,3-dihydroxybenzoyl)-L-serine
The 3 substrates of this enzyme are ATP, 2,3-dihydroxybenzoate, and L-serine, whereas its two products are products of ATP breakdown and N-(2,3-dihydroxybenzoyl)-L-serine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is 2,3-dihydroxybenzoate:L-serine ligase. Other names in common use include N-(2,3-dihydroxybenzoyl)-serine synthetase, and 2,3-dihydroxybenzoylserine synthetase.
References
[edit]- Brot N, Goodwin J (1968). "Regulation of 2,3-dihydroxybenzoylserine synthetase by iron". J. Biol. Chem. 243 (3): 510–3. doi:10.1016/S0021-9258(18)93633-1. PMID 4966114.
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