دورية أكاديمية
The mechanism of a one-substrate transketolase reaction.
| العنوان: | The mechanism of a one-substrate transketolase reaction. |
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| المؤلفون: | Solovjeva ON; Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russian Federation., Kovina MV; Advanced Cell Technologies Department, Sechenov First Moscow State Medical University (Sechenov University), Trubetskaya Street 8, 119991 Moscow, Russian Federation., Zavialova MG; Institute of Biomedical Chemistry, Pogodinskaya 10, 119121 Moscow, Russian Federation., Zgoda VG; Institute of Biomedical Chemistry, Pogodinskaya 10, 119121 Moscow, Russian Federation., Shcherbinin DS; Institute of Biomedical Chemistry, Pogodinskaya 10, 119121 Moscow, Russian Federation., Kochetov GA; Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russian Federation. |
| المصدر: | Bioscience reports [Biosci Rep] 2020 Aug 28; Vol. 40 (8). |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Portland Press on behalf of the Biochemical Society Country of Publication: England NLM ID: 8102797 Publication Model: Print Cited Medium: Internet ISSN: 1573-4935 (Electronic) Linking ISSN: 01448463 NLM ISO Abbreviation: Biosci Rep Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: London : Portland Press on behalf of the Biochemical Society Original Publication: London : The Biochemical Society, c1981- |
| مواضيع طبية MeSH: | Pentosephosphates/*metabolism , Pyruvates/*metabolism , Saccharomyces cerevisiae/*enzymology , Saccharomyces cerevisiae Proteins/*metabolism , Tetroses/*metabolism , Transketolase/*metabolism, Binding Sites ; Catalytic Domain ; Kinetics ; Molecular Dynamics Simulation ; Pentosephosphates/chemistry ; Protein Binding ; Protein Conformation ; Pyruvates/chemistry ; Saccharomyces cerevisiae Proteins/chemistry ; Spectrometry, Mass, Electrospray Ionization ; Structure-Activity Relationship ; Substrate Specificity ; Tandem Mass Spectrometry ; Tetroses/chemistry ; Transketolase/chemistry |
| مستخلص: | Transketolase catalyzes the transfer of a glycolaldehyde residue from ketose (the donor substrate) to aldose (the acceptor substrate). In the absence of aldose, transketolase catalyzes a one-substrate reaction that involves only ketose. The mechanism of this reaction is unknown. Here, we show that hydroxypyruvate serves as a substrate for the one-substrate reaction and, as well as with the xylulose-5-phosphate, the reaction product is erythrulose rather than glycolaldehyde. The amount of erythrulose released into the medium is equimolar to a double amount of the transformed substrate. This could only be the case if the glycol aldehyde formed by conversion of the first ketose molecule (the product of the first half reaction) remains bound to the enzyme, waiting for condensation with the second molecule of glycol aldehyde. Using mass spectrometry of catalytic intermediates and their subsequent fragmentation, we show here that interaction of the holotransketolase with hydroxypyruvate results in the equiprobable binding of the active glycolaldehyde to the thiazole ring of thiamine diphosphate and to the amino group of its aminopyrimidine ring. We also show that these two loci can accommodate simultaneously two glycolaldehyde molecules. It explains well their condensation without release into the medium, which we have shown earlier. (© 2020 The Author(s).) |
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| فهرسة مساهمة: | Keywords: mass-spectrometry; thiamine catalysis; transketolase |
| المشرفين على المادة: | 0 (Pentosephosphates) 0 (Pyruvates) 0 (Saccharomyces cerevisiae Proteins) 0 (Tetroses) 40031-31-0 (erythrulose) 60802-29-1 (xylulose-5-phosphate) 934B2KHY0S (hydroxypyruvic acid) EC 2.2.1.1 (Transketolase) |
| تواريخ الأحداث: | Date Created: 20180304 Date Completed: 20210330 Latest Revision: 20210330 |
| رمز التحديث: | 20240628 |
| مُعرف محوري في PubMed: | PMC7403953 |
| DOI: | 10.1042/BSR20180246 |
| PMID: | 29500317 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1573-4935 |
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| DOI: | 10.1042/BSR20180246 |