Skip to main content
PMC home page
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1996 Jan 1;24(1):132–136. doi: 10.1093/nar/24.1.132

A cholinesterase genes server (ESTHER): a database of cholinesterase-related sequences for multiple alignments, phylogenetic relationships, mutations and structural data retrieval.

X Cousin 1, T Hotelier 1, P Liévin 1, J P Toutant 1, A Chatonnet 1
PMCID: PMC145568  PMID: 8594562

Abstract

We have built a database of sequences phylogenetically related to cholinesterases (ESTHER) for esterases, alpha/beta hydrolase enzymes and relatives). These sequences define a homogeneous group of enzymes (carboxylesterases, lipases and hormone-sensitive lipases) with some related proteins devoid of enzymatic activity. The purpose of ESTHER is to help comparison and alignment of any new sequence appearing in the field, to favour mutation analysis of structure-function relationships and to allow structural data recovery. ESTHER is a World Wide Web server with the URL http://www.montpellier.inra.fr:70/cholinesterase.

Full Text

The Full Text of this article is available as a PDF (108.4 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. doi: 10.1016/S0022-2836(05)80360-2. [DOI] [PubMed] [Google Scholar]
  2. Arpagaus M., Chatonnet A., Masson P., Newton M., Vaughan T. A., Bartels C. F., Nogueira C. P., La Du B. N., Lockridge O. Use of the polymerase chain reaction for homology probing of butyrylcholinesterase from several vertebrates. J Biol Chem. 1991 Apr 15;266(11):6966–6974. [PubMed] [Google Scholar]
  3. Auld V. J., Fetter R. D., Broadie K., Goodman C. S. Gliotactin, a novel transmembrane protein on peripheral glia, is required to form the blood-nerve barrier in Drosophila. Cell. 1995 Jun 2;81(5):757–767. doi: 10.1016/0092-8674(95)90537-5. [DOI] [PubMed] [Google Scholar]
  4. Bairoch A., Boeckmann B. The SWISS-PROT protein sequence data bank: current status. Nucleic Acids Res. 1994 Sep;22(17):3578–3580. [PMC free article] [PubMed] [Google Scholar]
  5. Hein J. Unified approach to alignment and phylogenies. Methods Enzymol. 1990;183:626–645. doi: 10.1016/0076-6879(90)83041-7. [DOI] [PubMed] [Google Scholar]
  6. Hemilä H., Koivula T. T., Palva I. Hormone-sensitive lipase is closely related to several bacterial proteins, and distantly related to acetylcholinesterase and lipoprotein lipase: identification of a superfamily of esterases and lipases. Biochim Biophys Acta. 1994 Jan 3;1210(2):249–253. doi: 10.1016/0005-2760(94)90129-5. [DOI] [PubMed] [Google Scholar]
  7. Henikoff S., Henikoff J. G. Protein family classification based on searching a database of blocks. Genomics. 1994 Jan 1;19(1):97–107. doi: 10.1006/geno.1994.1018. [DOI] [PubMed] [Google Scholar]
  8. Ichtchenko K., Hata Y., Nguyen T., Ullrich B., Missler M., Moomaw C., Südhof T. C. Neuroligin 1: a splice site-specific ligand for beta-neurexins. Cell. 1995 May 5;81(3):435–443. doi: 10.1016/0092-8674(95)90396-8. [DOI] [PubMed] [Google Scholar]
  9. Jbilo O., Toutant J. P., Vatsis K. P., Chatonnet A., Lockridge O. Promoter and transcription start site of human and rabbit butyrylcholinesterase genes. J Biol Chem. 1994 Aug 19;269(33):20829–20837. [PubMed] [Google Scholar]
  10. Krejci E., Duval N., Chatonnet A., Vincens P., Massoulié J. Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid. Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6647–6651. doi: 10.1073/pnas.88.15.6647. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Massoulié J., Pezzementi L., Bon S., Krejci E., Vallette F. M. Molecular and cellular biology of cholinesterases. Prog Neurobiol. 1993 Jul;41(1):31–91. doi: 10.1016/0301-0082(93)90040-y. [DOI] [PubMed] [Google Scholar]
  12. Mutero A., Bride J. M., Pralavorio M., Fournier D. Drosophila melanogaster acetylcholinesterase: identification and expression of two mutations responsible for cold- and heat-sensitive phenotypes. Mol Gen Genet. 1994 Jun 15;243(6):699–705. doi: 10.1007/BF00279580. [DOI] [PubMed] [Google Scholar]
  13. Ollis D. L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S. M., Harel M., Remington S. J., Silman I., Schrag J. The alpha/beta hydrolase fold. Protein Eng. 1992 Apr;5(3):197–211. doi: 10.1093/protein/5.3.197. [DOI] [PubMed] [Google Scholar]
  14. Richardson D. C., Richardson J. S. The kinemage: a tool for scientific communication. Protein Sci. 1992 Jan;1(1):3–9. doi: 10.1002/pro.5560010102. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Schrag J. D., Li Y. G., Wu S., Cygler M. Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature. 1991 Jun 27;351(6329):761–764. doi: 10.1038/351761a0. [DOI] [PubMed] [Google Scholar]
  16. Schrag J. D., Winkler F. K., Cygler M. Pancreatic lipases: evolutionary intermediates in a positional change of catalytic carboxylates? J Biol Chem. 1992 Mar 5;267(7):4300–4303. [PubMed] [Google Scholar]
  17. Sussman J. L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 1991 Aug 23;253(5022):872–879. doi: 10.1126/science.1678899. [DOI] [PubMed] [Google Scholar]
  18. Talesa V., Culetto E., Schirru N., Bernardi H., Fedon Y., Toutant J. P., Arpagaus M. Characterization of a null mutation in ace-1, the gene encoding class A acetylcholinesterase in the nematode Caenorhabditis elegans. FEBS Lett. 1995 Jan 9;357(3):265–268. doi: 10.1016/0014-5793(94)01343-y. [DOI] [PubMed] [Google Scholar]
  19. Thompson J. D., Higgins D. G., Gibson T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994 Nov 11;22(22):4673–4680. doi: 10.1093/nar/22.22.4673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Winkler F. K., D'Arcy A., Hunziker W. Structure of human pancreatic lipase. Nature. 1990 Feb 22;343(6260):771–774. doi: 10.1038/343771a0. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES