NORINE: a database of nonribosomal peptides.
Norine is the first database entirely dedicated to nonribosomal peptides (NRPs). In bacteria and fungi, in addition to the traditional ribosomal proteic biosynthesis, an alternative ribosome-independent pathway called NRP synthesis allows peptide production. It is performed by huge protein complexes called nonribosomal peptide synthetases (NRPSs). The molecules synthesized by NRPS contain a high proportion of nonproteogenic amino acids. The primary structure of these peptides is not always linear but often more complex and may contain cycles and branchings. In recent years, NRPs attracted a lot of attention because of their biological activities and pharmacological properties (antibiotic, immunosuppressor, antitumor, etc.). However, few computational resources and tools dedicated to those peptides have been available so far. Norine is focused on NRPs and contains more than 700 entries. The database is freely accessible at http://bioinfo.lifl.fr/norine/. It provides a complete computational tool for systematic study of NRPs in numerous species, and as such, should permit to obtain a better knowledge of these metabolic products and underlying biological mechanisms, and ultimately to contribute to the redesigning of natural products in order to obtain new bioactive compounds for drug discovery.
Caboche
Ségolène
S
Computer Science Laboratory of Lille (UMR USTL/CNRS 8022) and INRIA, and ProBioGEM (UPRES EA 1026), University of Sciences and Technologies of Lille, 59655 Villeneuve d'A;scq, France. caboche@lifl.fr
Pupin
Maude
M
Leclère
Valérie
V
Fontaine
Arnaud
A
Jacques
Philippe
P
Kucherov
Gregory
G
D030562:Databases, Protein; D020407:Internet; D046908:Peptide Biosynthesis, Nucleic Acid-Independent; D010453:Peptide Synthases / Q000378:metabolism; D010455:Peptides / Q000737:chemistry*; D014584:User-Computer Interface
D010455:Peptides; D010453:Peptide Synthases; C104385:non-ribosomal peptide synthase