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Literature summary for 6.2.1.71 extracted from

  • Ehmann, D.; Shaw-Reid, C.; Losey, H.; Walsh, C.
    The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase Sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates (2000), Proc. Natl. Acad. Sci. USA, 97, 2509-2514 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli P10378
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2,3-dihydroxybenzoate + [aryl-carrier protein domain of EntB]
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Escherichia coli AMP + diphosphate + 2,3-dihydroxybenzoyl-[aryl-carrier protein domain of EntB]
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?
ATP + salicylate + holo-[aryl-carrier protein domain of EntB]
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Escherichia coli AMP + diphosphate + salicyl-[aryl-carrier protein domain of EntB]
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?
ATP + salicylate + holo-[aryl-carrier protein domain of SrfB1] SrfB1, i.e. peptidyl carrier protein of surfactin synthetase Escherichia coli AMP + diphosphate + salicyl-[aryl-carrier protein domain of SrfB1]
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?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.008
-
salicylate acceptor aryl-carrier protein domain of SrfB1, pH 7.5, 37°C Escherichia coli
2.15
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salicylate acceptor aryl-carrier protein domain of EntB, pH 7.5, 37°C Escherichia coli

General Information

General Information Comment Organism
physiological function enterobactin, the tris-(N-(2,3-dihydroxybenzoyl)serine) trilactone siderophore of Escherichia coli, is synthesized by a three-protein (EntE, B, F) six-module nonribosomal peptide synthetase Escherichia coli