2.7.4.2: phosphomevalonate kinase

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For detailed information about phosphomevalonate kinase, go to the full flat file.

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

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.4 Phosphotransferases with a phosphate group as acceptor

                2.7.4.2 phosphomevalonate kinase

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1	Activating Compound
6036	AA Sequence
2	Application
1	CAS Registry Number
18	Cloned(Commentary)
8	Cofactor
5	Crystallization (Commentary)
12	Disease/ Diagnostics
2	Expression
16	General Information
1	General Stability
29	Inhibitors
14	Ki Value [mM]
131	KM Value [mM]
7	Localization
41	Metals/Ions
16	Molecular Weight [Da]
23	Natural Substrates/ Products (Substrates)
42	Organism
1	Oxidation Stability
7	Pathway
8	PDB ID
9	pH Optimum
3	pH Range
1	pH Stability
2	pI Value
30	Protein Variants
16	Purification (Commentary)
7	Reaction
4	Reaction Type
41	Reference
26	Source Tissue
7	Specific Activity [micromol/min/mg]
6	Storage Stability
63	Substrates and Products (Substrate)
16	Subunits
44	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
2	Temperature Stability [°C]
4	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.4.2 - phosphomevalonate kinase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

1.8 A resolution. Molecule exhibits a compact alpha/beta structure and shows a sulfate molecule tightly bound to the P-loop. This sulfate ion forms hydrogen bonds with the amino group of amino acid G21 and with the side chain of R141

Homo sapiens

Q15126

695060

NMR-based dynamics and chemical shift experiments of enzyme in complex with MgADP, mevalonate 5-phosphate and the ternary complex. Binding of mevalonate 5-phosphate causes the protein to compress, whereas subsequent binding of MgADP opens the structure. Mevalonate 5-phosphate causes movement around a hinge region to permit domain closure. Amino acids H55 and R93 may act as hinge residues, D163 may be a hinge residue for the lid region. Binding of ATP or ADP causes similar conformational changes. The first nine residues of the N-terminus are highly disordered

Homo sapiens

-

695050

purified recombinant His6-tagged enzyme, mixing of 0.002 ml of 10 mg/mL protein in 100 mM (NH4)2SO4, 20 mM HEPES, pH 7.6, with 0.002 ml reservoir solution containing 15% v/v pentaerythritol ethoxylate, 100 mM HEPES, pH 7.6, 15% v/v MPD, 15°C, 2-3 days, X-ray diffraction structure determination and analysis at 1.76 A resolution, SAD method

Homo sapiens

-

710506

enzyme in a ternary complex with phosphomevalonate, AMPPNP, and Mg2+, by sitting drop method, mixing 0.002 ml of 12 mg/ml PMK in 25 mM HEPES/K+, pH 7.5, 0.25 mM phosphomevalonate, 8 mM AMPPNP, 10 mM MgCl2, with 0.002 ml of 36% w/v PEG 4000, and 100 mM MES/Na+, pH 6.0, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement with EPMR

Streptococcus pneumoniae

-

707502

hanging-drop vapor diffusion at 20°C against a reservoir containing 100 mM HEPES pH 7.5, 800 mM NaH2PO4, 8000 mM KH2PO4 and 30 mM unbuffered ATP, crystals diffract to 2.4 A resolution

Streptococcus pneumoniae

-

645182