Multidomain enzymes involved in peptide synthesis
- 27 July 1992
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 307 (1) , 40-43
- https://doi.org/10.1016/0014-5793(92)80898-q
Abstract
Biosynthesis of peptides in non-ribosomal systems is catalyzed by multifunctional enzymes that employ the thio-template mechanism. Recent studies on the analysis of the primary structure of several peptide synthetases have revealed that they are organized in highly conserved and repeated functional domains. The aligned domains provide the template for peptide synthesis, and their order determines the sequence of the peptide product.Keywords
This publication has 36 references indexed in Scilit:
- Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate‐forming enzymesMolecular Microbiology, 1992
- Biosynthesis of the Escherichia coli siderophore enterobactin: sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheineBiochemistry, 1991
- Nonribosomal biosynthesis of peptide antibioticsEuropean Journal of Biochemistry, 1990
- On the domain construction of the multienzyme gramicidin S synthetase 2European Journal of Biochemistry, 1990
- The proline‐activating activity of the multienzyme gramicidin S synthetase 2 can be recovered on a 115‐kDa tryptic fragmentEuropean Journal of Biochemistry, 1990
- Molecular Biology of Antibiotic Production in BacillusCritical Reviews in Biotechnology, 1990
- Peptide Antibiotics, β-Lactams, and Related CompoundsCritical Reviews in Biotechnology, 1988
- Biosynthesis of Peptide AntibioticsAnnual Review of Microbiology, 1987
- Biosynthesis of Small PeptidesAnnual Review of Biochemistry, 1974
- Nonribosomal polypeptide synthesis on polyenzyme templatesAccounts of Chemical Research, 1973