Direct hydroxide attack is a plausible mechanism for amidase antibody 43C9
Copyright 2003 Wiley Periodicals, Inc. J Comput Chem 24: 1371-1377, 2003
| Veröffentlicht in: | Journal of computational chemistry. - 1984. - 24(2003), 12 vom: 01. Sept., Seite 1371-7 |
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| Weitere Verfasser: | , , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2003
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| Zugriff auf das übergeordnete Werk: | Journal of computational chemistry |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Antibodies, Catalytic Hydroxyl Radical 3352-57-6 Histidine 4QD397987E Amidohydrolases mehr... |
| Zusammenfassung: | Copyright 2003 Wiley Periodicals, Inc. J Comput Chem 24: 1371-1377, 2003 Direct hydroxide attack on the scissile carbonyl of the substrate has been suggested as a likely mechanism for esterase antibodies elicited by phosphonate haptens, which mimic the transition states for the alkaline hydrolysis of esters.1 The unique amidase activity of esterase antibody 43C9 has been attributed to nucleophilic attack by an active-site histidine residue.2 Yet, the active site of 43C9 is strikingly similar to those of other esterase antibodies, particularly 17E8. We have carried out quantum mechanical calculations, molecular dynamics simulations, and free energy calculations to assess the mechanism involving direct hydroxide attack for 43C9. Results support this mechanism and suggest that the mechanism is plausible for other antiphosphonate antibodies that catalyze the hydrolysis of (p-nitro)phenyl esters |
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| Beschreibung: | Date Completed 24.02.2004 Date Revised 21.11.2013 published: Print Citation Status MEDLINE |
| ISSN: | 1096-987X |