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Escherichia coli K-12 substr. MG1655 Protein Class: a non-ribosomal peptide synthetase

Abbrev Name: non-ribosomal peptide synthetase

Summary:
The biosynthetic system for the production of a non-ribosomal peptide operates nucleic acid-free at the protein level. The specific condensation of amino acids and related carboxyl containing compounds is directed by protein templates, and each biosynthetic step generally requires a protein module. A minimal configuration consists of an adenylation domain for amino acid activation, a thiolation domain for transfer of activated intermediates, and a condensation domain.

Domains and modules are assembled at the gene level into gene clusters, which are translated into multifunctional proteins or multi-enzyme complexes, and post-translationally modified by addition of 4'-phosphopantetheine to the thiolation domain [Welker06].

Since a minimal module requires 3-3.5 kbp of genetic sequence, and since most non-ribosomal peptide synthetases (NRPSs) consist of several such modules, some NRPS genes are the largest known genes [Finking04].

a non-ribosomal peptide synthetase compound structure

Child Classes: a gramicidin-S synthetase (0) , a PchE non-ribosomal peptide synthase protein (0) , a PchF non-ribosomal peptide synthase protein (0)

Instances:
2,3-dihydroxybenzoyl-EntB

SMILES: CC(C)(COP(=O)([O-])OCC(N[a non-ribosomal peptide synthetase])C(=O)[a non-ribosomal peptide synthetase])C(O)C(=O)NCCC(=O)NCCS

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [an acyl-carrier protein + coenzyme A → adenosine 3',5'-bisphosphate + a holo-[acyl-carrier protein] + H+] (2.7.8.7):
i1: [EntB aryl-carrier protein] + coenzyme A → a holo EntB isochorismatase/aryl-carrier protein + adenosine 3',5'-bisphosphate + H+ (2.7.8.7)

Credits:
Created 11-Sep-2008 by Caspi R , SRI International


References

Finking04: Finking R, Marahiel MA (2004). "Biosynthesis of nonribosomal peptides1." Annu Rev Microbiol 58;453-88. PMID: 15487945

Welker06: Welker M, von Dohren H (2006). "Cyanobacterial peptides - nature's own combinatorial biosynthesis." FEMS Microbiol Rev 30(4);530-63. PMID: 16774586


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Tue Jun 2, 2015, biocyc14.