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

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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Weise, C. Hucho, F. Raba, R. Aaviksaar, A. Kreienkamp, H. J.
Description	Author Affiliation: Kreienkamp HJ ( Institut für Biochemie, Freie Universität Berlin, Federal Republic of Germany.);
Abstract	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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	14
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetylcholinesterase Metabolism Cobra Venoms Electric Organ Affinity Labels Amino Acid Sequence Animals Aziridines Binding Sites Chromatography, High Pressure Liquid Kinetics Molecular Sequence Data Peptide Fragments Isolation & Purification Propidium Pharmacology Sequence Homology, Nucleic Acid Torpedo Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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