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Updated: Aug 4, 2026

Steady-state, Pre-steady-state, and Single-turnover Kinetic Measurement for DNA Glycosylase Activity
Published on: August 19, 2013
Enzyme catalysis: a new definition accounting for noncovalent substrate- and product-like states
1Dept 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
Abstract:
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.
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