Anionic subsites of the catalytic center of acetyl...[Proc Natl Acad Sci U S A. 1991]

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1: Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6117-21. Links

Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom.

Kreienkamp HJ, Weise C, Raba R, Aaviksaar A, Hucho F.

Institut für Biochemie, Freie Universität Berlin, Federal Republic of Germany.

A peptide of acetylcholinesterase (AcChoEase; acetylcholine acetylhydrolase, EC 3.1.1.7) from the venom of the cobra Naja naja oxiana labeled by the affinity reagent N,N-dimethyl-2-phenylaziridinium (DPA) has been identified. The sequence is Gly-Ala-Glu-Met-Trp-Asn-Pro-Asn. In AcChoEase from Torpedo californica, a homologous peptide was labeled and isolated. Its sequence is Ser-Gly-Ser-Glu-Met-Trp-Asn-Pro-Asn, representing positions 79 through 87. In both cases labeling can be prevented by 0.1 mM edrophonium, indicating that the respective peptides form part of the anionic subsite of the catalytic center. The modified residue was tryptophan (Trp-84 in Torpedo AcChoEase) in both enzymes. In contrast to AcChoEase from Torpedo, the enzyme from cobra venom does not contain a peripheral anionic binding site.

PMID: 2068091 [PubMed - indexed for MEDLINE]

PMCID: PMC52033

Anionic subsites of the acetylcholinesterase from Torpedo californica: affinity labelling with the cationic reagent N,N-dimethyl-2-phenyl-aziridinium.
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[EMBO J. 1990]
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[Proc Natl Acad Sci U S A. 1993]
Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis.
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[Proc Natl Acad Sci U S A. 1992]
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[Eur J Biochem. 1994]
ReviewSubstrate-binding sites in acetylcholinesterase.
Trends Pharmacol Sci. 1991 Nov; 12(11):422-6.

[Trends Pharmacol Sci. 1991]
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Cited by 2 PubMed Central articles

Identification of amino acid residues involved in the binding of Huperzine A to cholinesterases.
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[Protein Sci. 1994]
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[EMBO J. 1992]

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