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Literature summary extracted from

  • Bazaes, S.; Beytia, E.; Jabalquinto, A.M.; Solis de Ovando, F.; Gomez, I.
    Pig liver phosphomevalonate kinase. 2. Participation of cysteinyl and lysyl groups in catalysis (1980), Biochemistry, 19, 2305-2310.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.4.2 5,5'-dithiobis(2-nitrobenzoate) 0.1 mM, almost complete inactivation after 5 min, phosphomevalonate partially protects, inactivation is reverted by 2-mercaptoethanol or dithiothreitol Sus scrofa
2.7.4.2 pyridoxal 5'-phosphate 0.5 mM, 80% inactivation after 30 min, phosphomevalonate protects Sus scrofa
2.7.4.2 pyridoxamine 5'-phosphate 0.25 mM, 60% inactivation after 20 min Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.4.2 0.0082
-
 phosphomevalonate pH 7.5, 30°C Sus scrofa
2.7.4.2 0.256
-
 ATP pH 7.5, 30°C Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.2 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.4.2 liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.2 ATP + 5-phosphomevalonate
-
 Sus scrofa ADP + 5-diphosphomevalonate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.4.2 30
-
 assay at Sus scrofa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.4.2 10.2
-
 phosphomevalonate pH 7.5, 30°C Sus scrofa