Structure-Functional Examination of Novel Ribonucleoside Hydrolase C (RihC) from Limosilactobacillus reuteri LR1
Leonid A Shaposhnikov1,2, Natalia Yu Chikurova1,2, Denis L Atroshenko1,2,3
1Bach Institute of Biochemistry, Federal Research Centre "Fundamentals of Biotechnology" of the Russian Academy of Sciences, Leninsky Avenue, 33/2, Moscow 119071, Russia.
International Journal of Molecular Sciences
|January 11, 2024
Summary
Limosilactobacillus reuteri
Area of Science:
- Biochemistry
- Enzymology
- Structural Biology
Background:
- Ribonucleoside hydrolase C (RihC) is an enzyme synthesized by lactobacilli in response to Klebsiella.
- RihC cleaves ribonucleosides into nitrogenous bases and ribose.
Purpose of the Study:
- To characterize the RihC enzyme from Limosilactobacillus reuteri LR1.
- To investigate its substrate specificity, thermal stability, and structure-function relationship.
Main Methods:
- Gene cloning and expression of RihC from L. reuteri LR1.
- Enzymatic activity assays with various nucleoside substrates.
- Thermal stability analysis and X-ray crystallography.
- Comparative structural analysis of RihC from different species.
Main Results:
- The L. reuteri LR1 RihC enzyme is active towards ribonucleosides and arabinoside, with uridine as the preferred substrate.
- The enzyme exhibits tetrameric architecture.
- Structural analysis revealed correlations between RihC structure and enzymatic activity.
- Key structural motifs crucial for enzyme function were identified.
Conclusions:
- The study provides a comprehensive characterization of L. reuteri LR1 RihC.
- Structural insights enhance understanding of RihC enzyme family function.
- Identified structural motifs can guide future enzyme engineering efforts.
Keywords:
crystal structureenzymatic activitylactobacillimodel structure studiesnosocomial infectionsribonucleoside hydrolase CMore Related Videos
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