Gene_Locus Report

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Gene_locus Report for: torma-ACHE

Torpedo marmorata (Marbled electric ray) acetylcholinesterase

Comment
Alternate Cterminus: T or H peptide


Relationship
Family|ACHE
Block| C
Position in NCBI Life Tree|Torpedo marmorata
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Chondrichthyes: N E > Elasmobranchii: N E > Batoidea: N E > Torpediniformes: N E > Torpedinidae: N E > Torpedo: N E > Torpedo marmorata: N E


Molecular evidence
Database
36 mutations: Table (e.g. : C231A, C231S/L282A, C231S/N280Q/L282S ... more)
No structure
Kinetic: torma-ACHE





2 substrates: Acetylcholine, Acetylthiocholine
No inhibitor
1 Genbank : X05497
1 UniProt : P07692
1 Ncbi-nid : 64414
1 UniProt : P07692
1 Interpro : P07692
1 Prodom : P07692
1 Pfam : P07692
1 PIRSF : P07692
1 SUPERFAM : P07692
Sequence
Graphical view for this peptide sequence: torma-ACHE
Colored MSA for ACHE (raw)
DDDSELLVNTKSGKVMRTRIPVLSSHISAFLGIPFAEPPVGNMRFRRPEP
KKPWSGVWNASTYPNNCQQYVDEQFPGFPGSEMWNPNREMSEDCLYLNIW
VPSPRPKSATVMLWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRV
GAFGFLALHGSQEAPGNMGLLDQRMALQWVHDNIQFFGGDPKTVTLFGES
AGRASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELRR
NLNCNLNSDEDLIQCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEF
FPTSLESMLNAGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISRE
DFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNV
ICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGL
PLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQ
KFIDLNTEPIKVHQRLRVQMCVFWNQFLPKLLNATETIDEAERQWKTEFH
RWSSYMMHWKNQFDQYSRHENCAEL
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

DDDSELLVNTKSGKVMRTRIPVLSSHISAFLGIPFAEPPVGNMRFRRPEP
KKPWSGVWNASTYPNNCQQYVDEQFPGFPGSEMWNPNREMSEDCLYLNIW
VPSPRPKSATVMLWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRV
GAFGFLALHGSQEAPGNMGLLDQRMALQWVHDNIQFFGGDPKTVTLFGES
AGRASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELRR
NLNCNLNSDEDLIQCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEF
FPTSLESMLNAGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISRE
DFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNV
ICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGL
PLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQ
KFIDLNTEPIKVHQRLRVQMCVFWNQFLPKLLNATETIDEAERQWKTEFH
RWSSYMMHWKNQFDQYSRHENCAEL


References
    Title: Kinetics of Torpedo californica acetylcholinesterase inhibition by bisnorcymserine and crystal structure of the complex with its leaving group
    Bartolucci C, Stojan J, Yu QS, Greig NH, Lamba D
    Ref: Biochemical Journal, 444:269, 2012 : PubMed

            

    Title: cDNA sequences of Torpedo marmorata acetylcholinesterase: primary structure of the precursor of a catalytic subunit; existence of multiple 5'-untranslated regions
    Sikorav JL, Krejci E, Massoulie J
    Ref: EMBO Journal, 6:1865, 1987 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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