Document Detail


Functional maps of the junctions between interglobular contacts and active sites in glycolytic enzymes -- a comparative analysis of the biochemical and structural data.
MedLine Citation:
PMID:  11951058     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Oligomers and separate subunits of the glycolytic enzymes often have different catalytic properties. However, spectral data show an apparent lack of significant conformational changes 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: Analysis of the spatial structures of the junctions between interglobular contacts and binding sites may give a clue to the mechanism(s) of the activation. In this work, the problem was studied using available structural and biochemical data for the oligomeric enzymes of glycolysis. RESULTS: Computational analysis of the structures of the junctions has identified three structurally distinct types of junctions: 1. interglobular binding site (2 of 8 enzymes); 2. domain-domain stabilization (5 of 8); and 3. 'sequence overlap' or a local conformational change (all enzymes). Thus the catalytic activity may be influenced through the shifts 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, which suggests their biological importance. CONCLUSIONS: The results suggest that a profound and a complex change in conformation in subunits of an oligomeric enzyme may not be necessary for a significant change in the catalytic properties. The analysis maps the residues important for the junctions and thus for the link between the catalytic activity and the oligomeric state of the enzymes.
Authors:
Ivan Y Torshin
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Medical science monitor : international medical journal of experimental and clinical research     Volume:  8     ISSN:  1234-1010     ISO Abbreviation:  Med. Sci. Monit.     Publication Date:  2002 Apr 
Date Detail:
Created Date:  2002-04-12     Completed Date:  2002-09-26     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9609063     Medline TA:  Med Sci Monit     Country:  Poland    
Other Details:
Languages:  eng     Pagination:  BR123-35     Citation Subset:  IM    
Affiliation:
Laboratory of Kinetics and Catalysis, Chemical Department of Moscow State University, Moscow, Russia. biotiy@suez.cs.gsu.edu
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MeSH Terms
Descriptor/Qualifier:
Animals
Binding Sites
Catalysis
Computational Biology
Enzyme Activation
Escherichia coli Proteins / chemistry
Fructose-Bisphosphate Aldolase / chemistry
Glucose-6-Phosphate Isomerase / chemistry
Glyceraldehyde-3-Phosphate Dehydrogenases / chemistry
Glycolysis*
Holoenzymes / chemistry
Humans
Models, Molecular
Nephropidae
Phosphofructokinases / chemistry
Phosphoglycerate Mutase / chemistry
Phosphopyruvate Hydratase / chemistry
Protein Conformation*
Protein Interaction Mapping*
Protein Structure, Tertiary
Protein Subunits
Pyruvate Kinase / chemistry
Rabbits
Rats
Saccharomyces cerevisiae Proteins / chemistry
Structure-Activity Relationship
Triose-Phosphate Isomerase / chemistry
Chemical
Reg. No./Substance:
0/Escherichia coli Proteins; 0/Holoenzymes; 0/Protein Subunits; 0/Saccharomyces cerevisiae Proteins; EC 1.2.1.-/Glyceraldehyde-3-Phosphate Dehydrogenases; EC 2.7.1 -/Phosphofructokinases; EC 2.7.1.40/Pyruvate Kinase; EC 4.1.2.13/Fructose-Bisphosphate Aldolase; EC 4.2.1.11/Phosphopyruvate Hydratase; EC 5.3.1.1/Triose-Phosphate Isomerase; EC 5.3.1.9/Glucose-6-Phosphate Isomerase; EC 5.4.2.1/Phosphoglycerate Mutase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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