title: Chemical modification of allosteric properties of enzymes.
abstract: Chemical modification is usually employed to study enzyme active sites. Valuable information can also be obtained, however, when this technique is used to probe allosteric sites. This approach is discussed in this article, and it is exemplified in chemical modification studies of the allosteric enzyme phosphofructokinase.
authors.affiliation: Department of Biological Chemistry, University of Health Sciences, Chicago Medical School, Illinois, USA.
authors.forename: R G
authors.initials: RG
authors.lastname: Kemp
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry; D000494:Allosteric Regulation / Q000502:physiology*; D000495:Allosteric Site / Q000502:physiology*; D002951:Citrates / Q000737:chemistry; D004789:Enzyme Activation / Q000502:physiology*; D005632:Fructose / Q000737:chemistry; D008024:Ligands; D016297:Mutagenesis, Site-Directed / Q000502:physiology*; D010732:Phosphofructokinase-1 / Q000737:chemistry*; D011487:Protein Conformation; D013438:Sulfhydryl Compounds / Q000737:chemistry*
chemical_list: D002951:Citrates; D008024:Ligands; D013438:Sulfhydryl Compounds; D005632:Fructose; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1