Folding and association of oligomeric enzymes.
The spontaneous structure formation of oligomeric enzymes consists of the consecutive 'folding' and association of the constituent polypeptide chains. Whether catalytic function is an intrinsic property of the folded monomers may be determined using kinetic reconstitution experiments. It is shown that full activity requires association; the correct assembly of subunits depends on their proper folding. The native structure is determined as the kinetically accessible state of lowest free energy.
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000818:Animals; D004798:Enzymes / Q000378:metabolism; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D007527:Isoenzymes; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D046911:Macromolecular Substances; D008291:Malate Dehydrogenase / Q000378:metabolism; D010455:Peptides; D011487:Protein Conformation; D011489:Protein Denaturation; D013816:Thermodynamics
D004798:Enzymes; D007527:Isoenzymes; D046911:Macromolecular Substances; D010455:Peptides; D000429:Alcohol Oxidoreductases; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005634:Fructose-Bisphosphate Aldolase