Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.36 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
Search for more literature for 2.7.1.36

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rattus norvegicus

Protein Variants

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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