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Trp82 and Tyr332 Are Involved in Two Quaternary Ammonium Binding Domains of Human Butyrylcholinesterase as Revealed by Photoaffinity Labeling with [3H]DDF

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    Article

    Trp82 and Tyr332 Are Involved in Two Quaternary Ammonium Binding Domains of Human Butyrylcholinesterase as Revealed by Photoaffinity Labeling with [3H]DDF†
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    Laboratoire de Chimie Bio-organique, UMR 7514 CNRS, Faculté de Pharmacie, Université Louis Pasteur Strasbourg, 74 route du Rhin, BP 24, 67401 Illkirch Cedex, France, and Laboratoire de Spectrométrie de Masse Bio-organique, UMR 7509 CNRS, Faculté de Chimie, Université Louis Pasteur Strasbourg, 1 rue Blaise Pascal, 67096 Strasbourg Cedex, France
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    Biochemistry

    Cite this: Biochemistry 1998, 37, 29, 10507–10513
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    https://doi.org/10.1021/bi980536l
    Published June 26, 1998
    Copyright © 1998 American Chemical Society
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    Abstract

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    Purified butyrylcholinesterase (BuChE) was photolabeled by [3H]-p-N,N-dimethylamino benzene diazonium ([3H]DDF) to identify the quaternary ammonium binding sites on this protein [Ehret-Sabatier, L., Schalk, I., Goeldner, M., and Hirth, C. (1992) Eur. J. Biochem.203, 475−481]. The covalent photoincorporation occurs with a stoichiometry of one mole of probe per mole of inactivated site and could be fully prevented by several cholinergic inhibitors such as tacrine or tetramethylammonium. After complete deglycosylation of the enzyme using N-glycosidase F, the alkylated protein was trypsinolyzed and the digests were analyzed by HPLC coupled to ES-MS. A direct comparison of tryptic fragments from labeled and unlabeled BuChE allowed us to identify the tryptic peptide Tyr61-Lys103 as carrying the probe. Purification of the labeled peptides by anion-exchange chromatography gave a major radioactive peak which was further fractionated by reversed-phase HPLC leading to three, well-resolved, radioactive peaks. Microsequencing revealed that two of these peaks contained an overlapping sequence starting at Tyr61, while the third peak contained a sequence extending from Thr315. Radioactive signals could be unambiguously attributed to positions corresponding to residues Trp82 and Tyr332. This labeling study establishes the existence of two different binding domains for quaternary ammonium in BuChE and exemplifies additional cation/π interactions in cholinergic proteins. This work strongly supports the existence of a peripheral anionic site in BuChE, implying residue Tyr332 as a key element.

    Copyright © 1998 American Chemical Society

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    †

     This work was supported by the Centre National de la Recherche Scientifique, the Ministère de la Recherche et de la Technologie, and the European Community Biotechnology Program under Grant No. 960081.

    ‡

     Laboratoire de Chimie Bio-organique.

    §

     Laboratoire de Spectrométrie de Masse Bio-organique.

    *

     To whom correspondence should be adressed. E-mail:  goeldner@ bioorga.u-strasbg.fr.

    Cited By

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    Biochemistry

    Cite this: Biochemistry 1998, 37, 29, 10507–10513
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bi980536l
    Published June 26, 1998
    Copyright © 1998 American Chemical Society
    Request reuse permissions

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