Journal
METABOLIC ENGINEERING
Volume 3, Issue 1, Pages 78-95Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/mben.2000.0171
Keywords
-
Categories
Funding
- NCI NIH HHS [CA78747] Funding Source: Medline
- NIAID NIH HHS [AI40475] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA078747] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R29AI040475] Funding Source: NIH RePORTER
Ask authors/readers for more resources
The structural and catalytic similarities between modular nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) inspired us to search for hybrid NRPS-PKS systems. By examining the biochemical and genetic data known to date for the biosynthesis of hybrid peptide-polyketide natural products, we show (1) that the same catalytic sites are conserved between the hybrid NRPS PKS and normal NRPS or PKS systems, although the ketoacyl synthase domain in NRPS/PKS hybrids is unique, and (2) that specific interpolypeptide linkers exist at both the G and N-termini of the NRPS and PKS proteins, which presumably play a critical role in facilitating the transfer of the growing peptide or polyketide intermediate between NRPS and PKS modules in hybrid NRPS-PKS systems, These findings provide new insights for intermodular communications in hybrid NRPS-PKS systems and should now be taken into consideration in engineering hybrid peptide-polyketide biosynthetic pathways for making Nobel unnatural natural products. (C) 2001 Academic Press.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available