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Q34234062-30E19B46-B508-484D-8A4E-A8841D6DB808
Q34234062-30E19B46-B508-484D-8A4E-A8841D6DB808
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http://www.wikidata.org/entity/statement/Q34234062-30E19B46-B508-484D-8A4E-A8841D6DB808
QM/MM analysis suggests that Alkaline Phosphatase (AP) and nucleotide pyrophosphatase/phosphodiesterase slightly tighten the transition state for phosphate diester hydrolysis relative to solution: implication for catalytic promiscuity in the AP supe
P2860
Q34234062-30E19B46-B508-484D-8A4E-A8841D6DB808
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34234062-30E19B46-B508-484D-8A4E-A8841D6DB808
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a1cb34c6c7ea2865b5778ca314b75224f27f52c0
P2860
Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis