2.7.1.185: mevalonate 3-kinase

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For detailed information about mevalonate 3-kinase, go to the full flat file.

Reaction

Synonyms

ATP:(R)-MVA 3-phosphotransferase, M3K, mevalonate 3-kinase, mevalonate-3-kinase, More, PtM3K, PTO1356, Ta1305, TacM3K

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.1 Phosphotransferases with an alcohol group as acceptor

                2.7.1.185 mevalonate 3-kinase

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Results	in table
3	AA Sequence
2	Application
5	Cloned(Commentary)
3	Crystallization (Commentary)
44	General Information
7	kcat/KM [mM/s]
8	KM Value [mM]
1	Metals/Ions
20	Natural Substrates/ Products (Substrates)
66	Organism
5	Pathway
3	pH Optimum
1	pH Range
45	Protein Variants
4	Purification (Commentary)
6	Reaction
20	Reference
46	Substrates and Products (Substrate)
2	Subunits
53	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Range [°C]
3	Temperature Stability [°C]
7	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.1.185 - mevalonate 3-kinase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified enzyme in complex with (R)-5-diphosphomevalonate and adenosine 5'-O-(3-thio)triphosphate or with (R)-5-diphosphomevalonate and ADP, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution

Saccharolobus solfataricus

-

759486

analysis of the substrate-complex crystal structure of TacM3K (PDB ID 4RKS)

Thermoplasma acidophilum

Q9HIN1

758668

hanging drop method, crystal structure of mevalonate-3-kinase in the apo form, and with bound substrates is determined and compared to mevalonate diphosphate decarboxylase structures. The crystal structure of mevalonate-3-kinase provides insight into the mechanism of mevalonate diphosphate decarboxylase. Despite sharing nearly identical overall folds, important active site differences are identified. Glu140 in the center of the mevalonate-3-kinase active site is responsible for binding mevalonate while excluding mevalonate 5-diphosphate, Arg185/Ser105 catalyze phosphate transfer, and an invariant Asp/Lys pair previously thought to be responsible for phosphorylation in mevalonate diphosphate decarboxylase, is missing in mevalonate-3-kinase and replaced by non-essential Thr275/Leu18. A model is proposed in which mevalonate-3-kinase and mevalonate diphosphate decarboxylase both phosphorylate by stabilizing a phosphotransfer transition state (mevalonate-3-kinase via Arg185/Ser105, mevalonate diphosphate decarboxylase via Lys188), suggesting the invariant Asp/Lys pair unique to mevalonate diphosphate decarboxylase may be critical for the decarboxylation step rather than phosphorylation

Thermoplasma acidophilum

Q9HIN1

730902