aCHEdb: the database system for ESTHER, the alpha/beta fold family of proteins and the Cholinesterase gene server
- PMID: 9399841
- PMCID: PMC147245
- DOI: 10.1093/nar/26.1.226
aCHEdb: the database system for ESTHER, the alpha/beta fold family of proteins and the Cholinesterase gene server
Abstract
Acetylcholinesterase belongs to a family of proteins, the alpha/beta hydrolase fold family, whose constituents evolutionarily diverged from a common ancestor and share a similar structure of a central beta sheet surrounded by alpha helices. These proteins fulfil a wide range of physiological functions (hydrolases, adhesion molecules, hormone precursors) [Krejci,E., Duval,N., Chatonnet,A., Vincens,P. and Massoulié,J. (1991) Proc. Natl. Acad. Sci. USA , 88, 6647-6651]. ESTHER (for esterases, alpha/beta hydrolase enzymes and relatives) is a database aimed at collecting in one information system, sequence data together with biological annotations and experimental biochemical results related to the structure-function analysis of the enzymes of the family. The major upgrade of the database comes from the use of a new database management system: aCHEdb which uses the ACeDB program designed by Richard Durbin and Jean Thierry-Mieg. It can be found at http://www.ensam.inra.fr/cholinesterase
Similar articles
-
The alpha/beta fold family of proteins database and the cholinesterase gene server ESTHER.Nucleic Acids Res. 1997 Jan 1;25(1):143-6. doi: 10.1093/nar/25.1.143. Nucleic Acids Res. 1997. PMID: 9016525 Free PMC article.
-
New friendly tools for users of ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins.Chem Biol Interact. 2005 Dec 15;157-158:339-43. doi: 10.1016/j.cbi.2005.10.100. Epub 2005 Nov 17. Chem Biol Interact. 2005. PMID: 16297901
-
Kinetic parameters of cholinesterase interactions with organophosphates: retrieval and comparison tools available through ESTHER database: ESTerases, alpha/beta Hydrolase Enzymes and Relatives.Chem Biol Interact. 1999 May 14;119-120:567-76. doi: 10.1016/s0009-2797(99)00071-x. Chem Biol Interact. 1999. PMID: 10421496
-
The ESTHER database on alpha/beta hydrolase fold proteins - An overview of recent developments.Chem Biol Interact. 2023 Sep 25;383:110671. doi: 10.1016/j.cbi.2023.110671. Epub 2023 Aug 13. Chem Biol Interact. 2023. PMID: 37582413 Review.
-
Alpha/beta hydrolase fold: an update.Protein Pept Lett. 2009;16(10):1137-48. doi: 10.2174/092986609789071298. Protein Pept Lett. 2009. PMID: 19508187 Review.
Cited by
-
A four-to-one association between peptide motifs: four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway.EMBO J. 1998 Nov 2;17(21):6178-87. doi: 10.1093/emboj/17.21.6178. EMBO J. 1998. PMID: 9799227 Free PMC article.
-
Maspardin is mutated in mast syndrome, a complicated form of hereditary spastic paraplegia associated with dementia.Am J Hum Genet. 2003 Nov;73(5):1147-56. doi: 10.1086/379522. Epub 2003 Oct 16. Am J Hum Genet. 2003. PMID: 14564668 Free PMC article.
-
Factor analysis of the sensitivity of insect cholinesterases to irreversible inhibitors and the structure of their active center.Dokl Biochem Biophys. 2009 Mar-Apr;425:117-9. doi: 10.1134/s1607672909020161. Dokl Biochem Biophys. 2009. PMID: 19496337 No abstract available.
-
ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins.Nucleic Acids Res. 2004 Jan 1;32(Database issue):D145-7. doi: 10.1093/nar/gkh141. Nucleic Acids Res. 2004. PMID: 14681380 Free PMC article.
-
ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions.Nucleic Acids Res. 2013 Jan;41(Database issue):D423-9. doi: 10.1093/nar/gks1154. Epub 2012 Nov 27. Nucleic Acids Res. 2013. PMID: 23193256 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources