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Q27656532-7A3EB384-6F19-4DD3-8D80-5A3C06621BBF
Q27656532-7A3EB384-6F19-4DD3-8D80-5A3C06621BBF
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http://www.wikidata.org/entity/statement/Q27656532-7A3EB384-6F19-4DD3-8D80-5A3C06621BBF
Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus
P2860
Q27656532-7A3EB384-6F19-4DD3-8D80-5A3C06621BBF
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http://www.wikidata.org/entity/statement/Q27656532-7A3EB384-6F19-4DD3-8D80-5A3C06621BBF
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093b79e3e6347f7ee7eb2fed3b3ac70ac475b4af
P2860
Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: temperature- and pH-dependence.