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) (less) C231A : Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase C231S/L282A : Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase C231S/N280Q/L282S : Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase C231S : Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase C537D : Residues in the C-Terminus of Torpedo californica Acetylcholinesterase Important for Modification into a Glycophospholipid Anchored Form C537G : Residues in the C-Terminus of Torpedo californica Acetylcholinesterase Important for Modification into a Glycophospholipid Anchored Form C537S : Residues in the C-Terminus of Torpedo californica Acetylcholinesterase Important for Modification into a Glycophospholipid Anchored Form C537T/D538T/G539T : Residues in the C-Terminus of Torpedo californica Acetylcholinesterase Important for Modification into a Glycophospholipid Anchored Form D326N/E327Q : Site-Directed Mutagenesis of Functional Residues in Torpedo Acetylcholinesterase D326N : Site-Directed Mutagenesis of Functional Residues in Torpedo Acetylcholinesterase D397N : Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid D93N : Structurally Important Residues in the Region Ser91 to Asn98 of Torpedo Acetylcholinesterase D93V : Residues important for folding and dimerisation of recombinant Torpedo californica acetylcholinesterase E327D : Site-Directed Mutagenesis of Functional Residues in Torpedo Acetylcholinesterase E327Q : Site-Directed Mutagenesis of Functional Residues in Torpedo Acetylcholinesterase E92L : Structurally Important Residues in the Region Ser91 to Asn98 of Torpedo Acetylcholinesterase E92Q : Residues important for folding and dimerisation of recombinant Torpedo californica acetylcholinesterase F288L/F290V : Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis G80C/C231S/V431C : Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function G80C/C231S : Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function G80C/V431C : Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function G80C : Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function L282S : Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase L282S : Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase N280Q/L282S : Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase N280Q : Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase R44E : Residues important for folding and dimerisation of recombinant Torpedo californica acetylcholinesterase R44K : Residues important for folding and dimerisation of recombinant Torpedo californica acetylcholinesterase S291G : Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase V129K/C231S : Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function V129K : Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function V129R/C231S : Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function V129R : Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function V431C/C231S : Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function V431C : Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function W279A : Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis 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 Pfam : P07692 1 PIRSF : P07692 1 SUPERFAM : P07692

Sequence

Peptide

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:

Bartolucci C, Stojan J, Yu QS, Greig NH, Lamba D

Ref:

444

PubMed

Title:

Sikorav JL, Krejci E, Massoulie J

Ref:

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.

For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page

webmaster

Acknowledgements and disclaimer