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Enzyme action: lock up your waters?: Water and active sites
Author(s) -
Adrian J. Lapthorn,
Nicholas C. Price
Publication year - 2008
Publication title -
the biochemist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.126
H-Index - 7
eISSN - 1740-1194
pISSN - 0954-982X
DOI - 10.1042/bio03004004
Subject(s) - nucleophile , macromolecule , enzyme , chemistry , lock (firearm) , hydrolysis , solvent , bound water , folding (dsp implementation) , active site , amino acid , biochemistry , combinatorial chemistry , organic chemistry , molecule , catalysis , electrical engineering , engineering , mechanical engineering
Water is thought of as the universal solvent for biological macromolecules, and its interaction with the different amino acid side chains of proteins determines their folding. Only a small proportion of the water associated with enzymes is tightly bound, but this can play crucial roles in determining the rates and specificities of reactions. Water itself is a relatively poor nucleophile, and enzymes can employ different strategies to facilitate hydrolytic reactions.

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