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Literature summary extracted from

  • Potter, D.; Wojnar, J.M.; Narasimhan, C.; Miziorko, H.M.
    Identification and functional characterization of an active-site lysine in mevalonate kinase (1997), J. Biol. Chem., 272, 5741-5746.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.36 expression in Escherichia coli Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.36 K13M 56fold decrease in activity Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.36 0.166
-
 ATP pH 7.0, 30°C, K13M mevalonate kinase Rattus norvegicus
2.7.1.36 0.288
-
 (R,S)-mevalonate pH 7.0, 30°C Rattus norvegicus
2.7.1.36 1.24
-
 ATP pH 7.0, 30°C Rattus norvegicus
2.7.1.36 2.88
-
 (R,S)-mevalonate pH 7.0, 30°C, K13M mutant mevalonate kinase Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.36 42000
-
 2 * 42000, SDS-PAGE Rattus norvegicus
2.7.1.36 83000
-
 stokes radius and partial specific volume Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.36 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.36 recombinant mevalonate kinase, Fast Q, Phenyl-agarose Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.36 ATP + mevalonate
-
 Rattus norvegicus ADP + phosphomevalonate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.36 dimer 2 * 42000, SDS-PAGE Rattus norvegicus