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Q42284276-425D0EDD-B117-4C26-AD63-B5D74F38E387
Q42284276-425D0EDD-B117-4C26-AD63-B5D74F38E387
BestRank
Statement
http://www.wikidata.org/entity/statement/Q42284276-425D0EDD-B117-4C26-AD63-B5D74F38E387
Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: temperature- and pH-dependence.
P2860
Q42284276-425D0EDD-B117-4C26-AD63-B5D74F38E387
BestRank
Statement
http://www.wikidata.org/entity/statement/Q42284276-425D0EDD-B117-4C26-AD63-B5D74F38E387
rank
NormalRank
type
BestRank
Statement
wasDerivedFrom
80ec24749089288be0e04bb4b2b8eb6f1c2ef742
P2860
Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues.