Title : The phosphorylation mechanism of mevalonate diphosphate decarboxylase: a QM/MM study.

Pub. Date : 2020 Jan 22

PMID : 31854421






4 Functional Relationships(s)
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1 Here by analogizing structurally related kinases and molecular dynamics simulations, we constructed a model of the MDD-substrate-ATP-Mg2+ complex and proposed that MDD requires two Mg2+ ions for maintaining a catalytically active conformation. Magnesium mevalonate diphosphate decarboxylase Homo sapiens
2 Here by analogizing structurally related kinases and molecular dynamics simulations, we constructed a model of the MDD-substrate-ATP-Mg2+ complex and proposed that MDD requires two Mg2+ ions for maintaining a catalytically active conformation. Magnesium mevalonate diphosphate decarboxylase Homo sapiens
3 Here by analogizing structurally related kinases and molecular dynamics simulations, we constructed a model of the MDD-substrate-ATP-Mg2+ complex and proposed that MDD requires two Mg2+ ions for maintaining a catalytically active conformation. Magnesium mevalonate diphosphate decarboxylase Homo sapiens
4 Here by analogizing structurally related kinases and molecular dynamics simulations, we constructed a model of the MDD-substrate-ATP-Mg2+ complex and proposed that MDD requires two Mg2+ ions for maintaining a catalytically active conformation. Magnesium mevalonate diphosphate decarboxylase Homo sapiens