The structure of ribose 5-phosphate isomerase from Plasmodium falciparum, PFE0730c, has been determined by molecular replacement at 2.09 angstroms resolution. The enzyme, which catalyzes the isomerization reaction that interconverts ribose 5-phosphate and ribulose 5-phosphate, is a member of the pentose phosphate pathway. The P. falciparum enzyme belongs to the ribose 5-phosphate isomerase A family, Pfam family PF06562 (DUF1124), and is structurally similar to other members of the family.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2219984 | PMC |
| http://dx.doi.org/10.1107/S1744309106010876 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Biophysical Characterization of a Novel Phosphopentomutase from the Hyperthermophilic Archaeon .
Int J Mol Sci
November 2024
School of Biological Sciences, University of the Punjab, Lahore 54590, Pakistan.
Phosphopentomutases catalyze the isomerization of ribose 1-phosphate and ribose 5-phosphate. , a hyperthermophilic archaeon, harbors a novel enzyme (PPM) that exhibits high homology with phosphohexomutases but has no significant phosphohexomutase activity. Instead, PPM catalyzes the interconversion of ribose 1-phosphate and ribose 5-phosphate.
View Article and Find Full Text PDFEvaluation of cross-linkers in the design of immobilized multi isomerase cascade for the preparation of rare sugars.
Int J Biol Macromol
December 2024
School of Chemistry and Life Sciences, Suzhou University of Science and Technology, Suzhou 215009, China. Electronic address:
The cascade of sugar isomerases is one of the most practical methods for producing rare sugars, and enzyme immobilization endows it with high economic efficiency, operational convenience and reusability. However, the most employed cross-linker glutaraldehyde (GA) has the disadvantages of enzyme deactivation and limitation of substrate binding. Herein, three compounds, glyoxal, GA, and 2,5-furandicarboxaldehyde (DFF) were evaluated within a previously developed cascade comprising ribose-5-phosphate isomerase and D-tagatose-3-epimerase to prepare D-ribulose form D-xylose.
View Article and Find Full Text PDFDisruptions of Genes Encoding Ribose-5-Phosphate Isomerases in Increases Sensitivity of Bacteria to Antibiotics.
Cells
November 2024
Engelhardt Institute of Molecular Biology, Russian Academy of Science, 119991 Moscow, Russia.
In cells, the main enzymes involved in pentose interconversion are ribose-5-phosphate isomerases RpiA and RpiB and ribulose-5-phosphate epimerase Rpe. The inactivation of limits ribose-5-phosphate (R5P) synthesis via the oxidative branch of the pentose phosphate pathway (PPP) and unexpectedly results in antibiotic supersensitivity. This type of metabolism is accompanied by significant changes in the level of reducing equivalents of NADPH and glutathione, as well as a sharp drop in the ATP pool.
View Article and Find Full Text PDFStructure and identification of the native PLP synthase complex from lysate.
mBio
November 2024
Department of Microbiology, Immunology & Molecular Genetics, University of California Los Angeles, Los Angeles, California, USA.
Many protein-protein interactions behave differently in biochemically purified forms as compared to their states. As such, determining native protein structures may elucidate structural states previously unknown for even well-characterized proteins. Here, we apply the bottom-up structural proteomics method, , toward a model methanogenic archaeon.
View Article and Find Full Text PDFCharacterization of a widespread sugar phosphate-processing bacterial microcompartment.
Commun Biol
November 2024
MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, USA.
Article Synopsis
- Prokaryotes utilize Bacterial Microcompartments (BMCs) to encapsulate metabolic pathways, enhancing enzyme activity for improved catalysis.
- Sugar Phosphate Utilizing (SPU) BMCs, present in various environments from soils to hot springs, are characterized by their unique enzyme, deoxyribose 5-phosphate aldolase (DERA).
- This study defines the key features of SPU BMCs, demonstrating the catalytic activity of DERA and its role as a signature enzyme, which could have significant implications for understanding their function and potential biotechnological uses.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!