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Q42284276-511C0965-6F14-497D-8B99-07D72F94EC9C
Q42284276-511C0965-6F14-497D-8B99-07D72F94EC9C
BestRank
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http://www.wikidata.org/entity/statement/Q42284276-511C0965-6F14-497D-8B99-07D72F94EC9C
Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: temperature- and pH-dependence.
P2860
Q42284276-511C0965-6F14-497D-8B99-07D72F94EC9C
BestRank
Statement
http://www.wikidata.org/entity/statement/Q42284276-511C0965-6F14-497D-8B99-07D72F94EC9C
rank
NormalRank
type
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Statement
wasDerivedFrom
7483a066c1822b03730c44966a5d72ed481c3cb5
P2860
Hydrolysis of phosphodiesters through transformation of the bacterial phosphotriesterase.