دورية أكاديمية
أعرض في EDS

Ribosome External Electric Field Regulates Metabolic Enzyme Activity: The RAMBO Effect.

التفاصيل البيبلوغرافية
العنوان: Ribosome External Electric Field Regulates Metabolic Enzyme Activity: The RAMBO Effect.
المؤلفون: Yu J; Department of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States., Ramirez LM; Department of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States., Lin Q; RNA Epitranscriptomics & Proteomics Resource, University at Albany, State University of New York, Albany, New York 12222, United States., Burz DS; Department of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States., Shekhtman A; Department of Chemistry, University at Albany, State University of New York, Albany, New York 12222, United States.
المصدر: The journal of physical chemistry. B [J Phys Chem B] 2024 Jul 25; Vol. 128 (29), pp. 7002-7021. Date of Electronic Publication: 2024 Jul 16.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101157530 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5207 (Electronic) Linking ISSN: 15205207 NLM ISO Abbreviation: J Phys Chem B Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Chemical Society, c1997-
مواضيع طبية MeSH: Triose-Phosphate Isomerase*/metabolism , Triose-Phosphate Isomerase*/chemistry , Ribosomes*/metabolism , Ribosomes*/chemistry, Ribosomal Proteins/metabolism ; Ribosomal Proteins/chemistry ; Kinetics ; Electricity ; Protein Binding
مستخلص: Ribosomes bind to many metabolic enzymes and change their activity. A general mechanism for ribosome-mediated amplification of metabolic enzyme activity, RAMBO, was formulated and elucidated for the glycolytic enzyme triosephosphate isomerase, TPI. The RAMBO effect results from a ribosome-dependent electric field-substrate dipole interaction energy that can increase or decrease the ground state of the reactant and product to regulate catalytic rates. NMR spectroscopy was used to determine the interaction surface of TPI binding to ribosomes and to measure the corresponding kinetic rates in the absence and presence of intact ribosome particles. Chemical cross-linking and mass spectrometry revealed potential ribosomal protein binding partners of TPI. Structural results and related changes in TPI energetics and activity show that the interaction between TPI and ribosomal protein L11 mediate the RAMBO effect.
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معلومات مُعتمدة: P01 HL146367 United States HL NHLBI NIH HHS; R01 GM085006 United States GM NIGMS NIH HHS; R01 GM143749 United States GM NIGMS NIH HHS
المشرفين على المادة: EC 5.3.1.1 (Triose-Phosphate Isomerase)
0 (Ribosomal Proteins)
تواريخ الأحداث: Date Created: 20240716 Date Completed: 20240725 Latest Revision: 20240731
رمز التحديث: 20240731
مُعرف محوري في PubMed: PMC11284791
DOI: 10.1021/acs.jpcb.4c00628
PMID: 39012038
قاعدة البيانات: MEDLINE
الوصف
تدمد:1520-5207
DOI:10.1021/acs.jpcb.4c00628