Enzyme catalysis: a new definition accounting for noncovalent substrate- and product-like states.
Biological catalysis frequently causes changes in noncovalent bonding. By building on Pauling's assertion that any long-lived, chemically distinct interaction is a chemical bond, this article redefines enzyme catalysis as the facilitated making and/or breaking of chemical bonds, not just of covalent bonds. It is also argued that nearly every ATPase or GTPase is misnamed as a hydrolase and actually belongs to a distinct class of enzymes, termed here 'energases'. By transducing covalent bond energy into mechanical work, energases mediate such fundamental processes as protein folding, self-assembly, G-protein interactions, DNA replication, chromatin remodeling and even active transport.
Purich
D L
DL
Dept of Biochemistry & Molecular Biology, PO Box 100245, College of Medicine, University of Florida Health Science Center, 1600 SW Archer Road, 32610-0245, Gainesville, FL, USA. dlpurich@biochem.med.ufl.edu
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D002384:Catalysis; D004798:Enzymes / Q000737:chemistry*; D020558:GTP Phosphohydrolases / Q000378:metabolism; D007700:Kinetics; D008956:Models, Chemical; D009154:Mutation; D011485:Protein Binding; D021381:Protein Transport; D013379:Substrate Specificity
D004798:Enzymes; D000251:Adenosine Triphosphatases; D020558:GTP Phosphohydrolases