دورية أكاديمية
Phosphate ions and glutaminyl cyclases catalyze the cyclization of glutaminyl residues by facilitating synchronized proton transfers.
| العنوان: | Phosphate ions and glutaminyl cyclases catalyze the cyclization of glutaminyl residues by facilitating synchronized proton transfers. |
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| المؤلفون: | Seifert F; Albrecht-von-Haller-Institute, University of Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany., Demuth HU; Probiodrug AG, Weinbergweg 22, 06120 Halle, Germany., Weichler T; Probiodrug AG, Weinbergweg 22, 06120 Halle, Germany., Ludwig HH; Probiodrug AG, Weinbergweg 22, 06120 Halle, Germany., Tittmann K; Albrecht-von-Haller-Institute, University of Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany., Schilling S; Probiodrug AG, Weinbergweg 22, 06120 Halle, Germany. Electronic address: Stephan.Schilling@izi.fraunhofer.de. |
| المصدر: | Bioorganic chemistry [Bioorg Chem] 2015 Jun; Vol. 60, pp. 98-101. Date of Electronic Publication: 2015 Apr 24. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 1303703 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1090-2120 (Electronic) Linking ISSN: 00452068 NLM ISO Abbreviation: Bioorg Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Amsterdam : Elsevier Original Publication: New York, London, Academic Press. |
| مواضيع طبية MeSH: | Aminoacyltransferases/*metabolism , Drosophila melanogaster/*enzymology , Phosphates/*metabolism , Pyrrolidonecarboxylic Acid/*metabolism, Animals ; Cyclization ; Drosophila melanogaster/metabolism ; Glutamine/metabolism ; Protons |
| مستخلص: | Phosphate ions and glutaminyl cyclase (QC) both catalyze the formation of pyroglutamate (pE, pGlu) from N-terminal glutamine residues of peptides and proteins. Here, we studied the mechanism of glutamine cyclization using kinetic secondary deuterium and solvent isotope effects. The data suggest that proton transfer(s) are rate determining for the spontaneous reaction, and that phosphate and QC are accelerating the reaction by promoting synchronized proton transfers in a concerted mechanism. Thus, non-enzymatic and enzymatic catalysis of pyroglutamate formation exploit a similar mode of transition-state stabilization. (Copyright © 2015 Elsevier Inc. All rights reserved.) |
| فهرسة مساهمة: | Keywords: 5-Oxo-l-proline; Acyl transfer; Glutamine; Pyroglutamic acid |
| المشرفين على المادة: | 0 (Phosphates) 0 (Protons) 0RH81L854J (Glutamine) EC 2.3.2.- (Aminoacyltransferases) EC 2.3.2.5 (glutaminyl-peptide cyclotransferase) SZB83O1W42 (Pyrrolidonecarboxylic Acid) |
| تواريخ الأحداث: | Date Created: 20150519 Date Completed: 20160229 Latest Revision: 20150605 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1016/j.bioorg.2015.04.005 |
| PMID: | 25981125 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1090-2120 |
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| DOI: | 10.1016/j.bioorg.2015.04.005 |