Source:
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: iGEM Marburg 2014
Date created: 2014-10-14 11:00:00
Date modified: 2015-05-08 01:09:55
NRPS: Amino acid activation domain
| Types | DnaRegion |
| Roles | engineered_region Device |
| Sequences | BBa_K1329005_sequence (Version 1) |
Description
This device is based on an already available part in the registry of standard biological parts: BBa_K1152005.Nonribosomal peptide synthetases (NRPSs) are a most fascinating subject because of the huge amount of biologically active compounds they produce that show a broad spectrum of clinical applications that even includes their use as last resort antibiotics, antitumor or antifungal agents and immunosuppressants. These interesting properties especially derive from the nonribosomal peptide synthetases unique feature to incorporate non-proteinogenic features such as heterocycles, fatty acids, macrocycles, D-amino acids and other non-proteinogenic amino acids. Last years??? team of the university Heidelberg used nonribosomal peptide synthetases of Brevibacillus parabrevis in order to synthesize a tripeptide by interchanging modules of an already existing NRPS cluster. The problem of previous applications such as these is that the size of synthesized peptides is limited. Even naturally occurring peptides synthesized nonribosomally seem to have an upper limit of 50 amino acids (Caboche et al., 2008). Therefore it would be great to establish a system that uses these capabilities to introduce non-proteinogenic amino acids but is able to overcome the size limit of the synthesized peptides. That is why we improved the brick BBa_K1152005 which contains the expression cassette for NRPS synthesizing a Phe-Orn-Leu-tripeptide. In RiboSURF, we improved the A-domain that activates phenylalanine in that nonribosomal peptide synthetase.