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Literature summary extracted from

  • Ishidate, K.; Furusawa, K.; Nakazawa, Y.
    Complete co-purification of choline kinase and ethanolamine kinase from rat kidney and immunological evidence for both kinase activities residing on the same enzyme protein(s) in rat tissues (1985), Biochim. Biophys. Acta, 836, 119-124.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.32 ethanolamine weak competitive inhibitor Rattus norvegicus
2.7.1.82 ATP concentration exceeding that of Mg2+ Rattus norvegicus
2.7.1.82 choline very strong Rattus norvegicus
2.7.1.82 Mn2+
-
Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.32 additional information
-
additional information Km of MgATP2-: 10 mM, in presence of equimolar amounts of ATP and Mg2+, 1.5 mM, in 2.5-fold higher concentration of Mg2+ than ATP Rattus norvegicus
2.7.1.82 additional information
-
additional information
-
Rattus norvegicus
2.7.1.82 1.5
-
ATP with 1.5-fold higher concentration of Mg2+ than ATP, pH 8.5 Rattus norvegicus
2.7.1.82 1.5
-
ATP ATP in form of MgATP2- Rattus norvegicus
2.7.1.82 10
-
ATP in presence of equivalent amounts of ATP and Mg2+, pH 8.5 Rattus norvegicus
2.7.1.82 10
-
ATP ATP in form of MgATP2- Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.32 cytosol
-
Rattus norvegicus 5829
-
2.7.1.82 cytosol
-
Rattus norvegicus 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.32 Mg2+ ATP concentration 1.25-2.5 mM: reaction requires free Mg2+ rather than MgATP2-, ATP concentration exceeding that of Mg2+: strong inhibition Rattus norvegicus
2.7.1.32 Mg2+ Km MgATP2-: 10 mM, in presence of equimolar amounts of ATP and Mg2+, Km MgATP2-: 1.5 mM, in 2.5 fold higher concentration of Mg2+ than ATP Rattus norvegicus
2.7.1.82 Mg2+ Km MgATP2-: 10 mM, in presence of equivalent amounts of ATP and Mg2+ Rattus norvegicus
2.7.1.82 Mg2+ 1.25-2.5 mM ATP: reaction requires free Mg2+ rather than an ATP-Mg2+ complex for maximal velocity Rattus norvegicus
2.7.1.82 Mg2+ 1.5 mM, in 1.5-fold higher concentration of Mg2+ than ATP Rattus norvegicus
2.7.1.82 Mg2+ ATP concentration exceeding that of Mg2+: strong inhibition Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.32 Rattus norvegicus
-
-
-
2.7.1.82 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.32 copurification of choline kinase and ethanolamine kinase Rattus norvegicus
2.7.1.82 copurification of choline kinase and ethanolamine kinase Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.32 ATP + choline = ADP + phosphocholine choline kinase and ethanolamine kinase may not have a common active site in a single enzyme protein Rattus norvegicus
2.7.1.82 ATP + ethanolamine = ADP + O-phosphoethanolamine choline kinase and ethanolamine kinase may not have a common active site in a single enzyme protein Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.82 kidney
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.32 1.5
-
-
Rattus norvegicus
2.7.1.82 1.398
-
pH 8.5 Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.32 ATP + choline
-
Rattus norvegicus ADP + O-phosphocholine
-
?
2.7.1.82 ATP + ethanolamine
-
Rattus norvegicus ADP + O-phosphoethanolamine
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.82 More cf. EC 2.7.1.32 Rattus norvegicus
2.7.1.82 More choline kinase and ethanolamine kinase may not have a common active site in a single enzyme protein Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.32 8.5 9
-
Rattus norvegicus
2.7.1.82 8 9
-
Rattus norvegicus