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Author(s) -
Keating Thomas A.,
Ehmann David E.,
Kohli Rahul M.,
Marshall C. Gary,
Trauger John W.,
Walsh Christopher T.
Publication year - 2001
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20010202)2:2<91::aid-cbic91>3.0.co;2-e
Subject(s) - nonribosomal peptide , enterobactin , siderophore , thioesterase , adenylylation , biosynthesis , escherichia coli , enzyme , chemistry , stereochemistry , serine , biochemistry , biology , gene
The cover picture shows a false‐color image of wild‐type Escherichia coli DH5(α) cells growing on an agar plate containing the indicator chromeazurol S. The siderophore enterobactin is secreted by iron‐starved colonies, resulting in Fe III ‐depleted, decolorized halos. The inset scheme shows the pathway for enterobactin biosynthesis from 2,3‐dihydroxybenzoic acid (2,3‐DHB) and L ‐serine by the nonribosomal peptide synthetase (NRPS) enzymes EntE, EntB, and EntF. These enzymes catalyze the formation of peptide bonds without mRNA templates and have a modular structure. A functional module consists of an adenylation (A), a thiolation (T), and a condensation (C) domain. The terminal thioesterase (TE) domain of EntF catalyzes elongation and cyclotrimerization to the final product. Further details about the diversity and function of the chain‐releasing C‐terminal domains of NRPS assembly lines can be found in the Minireview by C. T. Walsh et al. on p. 99 ff.