Article (Scientific journals)
NORINE: a database of nonribosomal peptides.
Caboche, Segolene; Pupin, Maude; Leclere, Valerie et al.
2008In Nucleic Acids Research, 36 (Database issue), p. 326-31
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Keywords :
Databases, Protein; Internet; Peptide Biosynthesis, Nucleic Acid-Independent; Peptide Synthases/metabolism; Peptides/chemistry; User-Computer Interface
Abstract :
[en] 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.
Disciplines :
Microbiology
Author, co-author :
Caboche, Segolene
Pupin, Maude
Leclere, Valerie
Fontaine, Arnaud
Jacques, Philippe ;  Université de Liège - ULiège > Chimie et bio-industries > Bio-industries
Kucherov, Gregory
Language :
English
Title :
NORINE: a database of nonribosomal peptides.
Publication date :
2008
Journal title :
Nucleic Acids Research
ISSN :
0305-1048
eISSN :
1362-4962
Publisher :
Oxford University Press, United Kingdom
Volume :
36
Issue :
Database issue
Pages :
D326-31
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 21 October 2014

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