2.7.4.2: phosphomevalonate kinase
This is an abbreviated version!
For detailed information about phosphomevalonate kinase, go to the full flat file.
Word Map on EC 2.7.4.2
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2.7.4.2
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isopentenyl
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isoprenoids
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diphosphomevalonate
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5-diphosphate
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mevalonate-5-pyrophosphate
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pyrophosphomevalonate
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2.7.1.36
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cholesterogenesis
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zellweger
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nonsterol
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medicine
- 2.7.4.2
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isopentenyl
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isoprenoids
- diphosphomevalonate
- 5-diphosphate
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mevalonate-5-pyrophosphate
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pyrophosphomevalonate
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2.7.1.36
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cholesterogenesis
-
zellweger
-
nonsterol
- medicine
Reaction
Synonyms
5-phosphomevalonate kinase, ATP:5-phosphomevalonate phosphotransferase, CcPMK, ERG8, GbPMK, kinase, phosphomevalonate (phosphorylating), mevalonate phosphate kinase, mevalonate-5-phosphate kinase, mevalonic acid phosphate kinase, More, phosphomevalonate kinase, phosphomevalonic kinase, PMK, PMVAK, PMVK, SSO2988
ECTree
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Reaction
Reaction on EC 2.7.4.2 - phosphomevalonate kinase
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sequential mechanism
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ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate
ordered mechanism
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ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate
kinetic mechanism, the enzyme follows hyperbolic kinetics and a sequential mechanism
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ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate
residue R110 is important to PMK catalysis, which is also influenced by K48 and R73. R111 and R84 contribute to binding of mevalonate 5-phosphate and R141 to binding of ATP
ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate
residue R22 is important for catalysis
ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate
the phosphorylation reaction mechanism of phosphomevalonate kinase is studied by using molecular dynamics and hybrid QM/MM methods, overview. A conserved residue (Ser106) is reorientated to anchor ATP via a stable H-bond interaction. In addition, Ser213 located on the alpha-helix at the catalytic site is repositioned to further approach the substrate, facilitating the proton transfer during the phosphorylation. Lys101 functions to neutralize the negative charge developed at the beta-, gamma-bridging oxygen atom of ATP during phosphoryl transfer
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