Enzyme catalysis: a new definition accounting for noncovalent substrate- and product-like states.
نویسنده
چکیده
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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ورودعنوان ژورنال:
- Trends in biochemical sciences
دوره 26 7 شماره
صفحات -
تاریخ انتشار 2001