01 January 2002
Functional maps of the junctions between interglobular contacts and activesites in glycolytic enzymes -- a comparative analysis of the biochemical and structural data.
Ivan Y TorshinMed Sci Monit 2002; 8(4): BR123-135 :: ID: 420880
Abstract
BACKGROUND: Oligomers and separate subunits of the glycolytic enzymes oftenhave different catalytic properties. However, spectral data show an apparent lack of significant conformationalchanges during oligomerization. Since the conformation of an enzyme determines its catalytic properties,the structural mechanism(s) influencing the activity is of considerable interest. MATERIAL/METHODS: Analysisof the spatial structures of the junctions between interglobular contacts and binding sites may givea clue to the mechanism(s) of the activation. In this work, the problem was studied using available structuraland biochemical data for the oligomeric enzymes of glycolysis. RESULTS: Computational analysis of thestructures of the junctions has identified three structurally distinct types of junctions: 1. interglobularbinding site (2 of 8 enzymes); 2. domain-domain stabilization (5 of 8); and 3. 'sequence overlap' ora local conformational change (all enzymes). Thus the catalytic activity may be influenced through theshifts of the modules of protein structure (types 1, 2) and/or due to a slight change in the local structure(type 3). The more common junctions of types 2 and 3 are well conserved among eukaryotic enzymes, whichsuggests their biological importance. CONCLUSIONS: The results suggest that a profound and a complexchange in conformation in subunits of an oligomeric enzyme may not be necessary for a significant changein the catalytic properties. The analysis maps the residues important for the junctions and thus forthe link between the catalytic activity and the oligomeric state of the enzymes.
Keywords: Binding Sites, Catalysis, Comparative Study, Computational Biology, Escherichia coli Proteins, Fructose-Bisphosphate Aldolase, Glucose-6-Phosphate Isomerase, Glyceraldehyde-3-Phosphate Dehydrogenases, Glycolysis, Holoenzymes, Models, Molecular, Nephropidae, Phosphofructokinases, phosphoglycerate mutase, Phosphopyruvate Hydratase, Protein Conformation, Protein Interaction Mapping, Protein Structure, Tertiary, Protein Subunits, Pyruvate Kinase, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship, Triose-Phosphate Isomerase
Editorial
01 March 2024 : Editorial
Editorial: First Regulatory Approvals for CRISPR-Cas9 Therapeutic Gene Editing for Sickle Cell Disease and Transfusion-Dependent β-ThalassemiaDOI: 10.12659/MSM.944204
Med Sci Monit 2024; 30:e944204
In Press
18 Mar 2024 : Clinical Research
Sexual Dysfunction in Women After Tibial Fracture: A Retrospective Comparative StudyMed Sci Monit In Press; DOI: 10.12659/MSM.944136
21 Feb 2024 : Clinical Research
Potential Value of HSP90α in Prognosis of Triple-Negative Breast CancerMed Sci Monit In Press; DOI: 10.12659/MSM.943049
22 Feb 2024 : Review article
Differentiation of Native Vertebral Osteomyelitis: A Comprehensive Review of Imaging Techniques and Future ...Med Sci Monit In Press; DOI: 10.12659/MSM.943168
23 Feb 2024 : Clinical Research
A Study of 60 Patients with Low Back Pain to Compare Outcomes Following Magnetotherapy, Ultrasound, Laser, ...Med Sci Monit In Press; DOI: 10.12659/MSM.943732
Most Viewed Current Articles
16 May 2023 : Clinical Research
Electrophysiological Testing for an Auditory Processing Disorder and Reading Performance in 54 School Stude...DOI :10.12659/MSM.940387
Med Sci Monit 2023; 29:e940387
17 Jan 2024 : Review article
Vaccination Guidelines for Pregnant Women: Addressing COVID-19 and the Omicron VariantDOI :10.12659/MSM.942799
Med Sci Monit 2024; 30:e942799
14 Dec 2022 : Clinical Research
Prevalence and Variability of Allergen-Specific Immunoglobulin E in Patients with Elevated Tryptase LevelsDOI :10.12659/MSM.937990
Med Sci Monit 2022; 28:e937990
01 Jan 2022 : Editorial
Editorial: Current Status of Oral Antiviral Drug Treatments for SARS-CoV-2 Infection in Non-Hospitalized Pa...DOI :10.12659/MSM.935952
Med Sci Monit 2022; 28:e935952