1. Interdomain interactions in oligomeric enzymes: creation of asymmetry in homo-oligomers and role in metabolite channeling between active centers of hetero-oligomers
- Author
-
Natalya K. Nagradova
- Subjects
Models, Molecular ,Stereochemistry ,Domain–domain interaction ,Metabolite ,media_common.quotation_subject ,Carbamoyl phosphate synthetase ,Biophysics ,D-Glyceraldehyde-3-phosphate dehydrogenase ,Carbamoyl-Phosphate Synthase (Ammonia) ,Dehydrogenase ,Tryptophan-tRNA Ligase ,In Vitro Techniques ,Biochemistry ,Asymmetry ,Conformational flexibility ,Geobacillus stearothermophilus ,chemistry.chemical_compound ,Structural Biology ,Tyrosine-tRNA Ligase ,Half-of-the-sites reactivity ,Metabolite channeling ,Genetics ,Escherichia coli ,Molecule ,Animals ,Pre-existent asymmetry in oligomeric protein ,Protein Structure, Quaternary ,Molecular Biology ,media_common ,chemistry.chemical_classification ,Tryptophanyl-tRNA synthetase ,Binding Sites ,Glyceraldehyde-3-Phosphate Dehydrogenases ,Cell Biology ,Enzymes ,Protein Structure, Tertiary ,Enzyme ,chemistry ,Intramolecular force ,Rabbits ,Function (biology) - Abstract
Interdomain interactions play an important role in the structural organization of many enzymes and the conformational flexibility of their molecules. In this review, the role of intrasubunit and intersubunit domain–domain interactions in the origins of pre-existent asymmetry of homo-oligomeric D -glyceraldehyde-3-phosphate dehydrogenase and tryptophanyl-tRNA synthetase is discussed on the basis of recent X-ray data and other available information about the properties of these and related enzymes. In addition, a novel key function of interdomain interactions is considered: their potential contribution to intramolecular channeling of intermediates between active centers located on different subunits of a hetero-oligomeric enzyme (α,β-heterodimeric carbamoyl phosphate synthetase).
- Published
- 2001