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Literature summary for 2.7.1.107 extracted from

  • Bohnenberger, E.; Sandermann, H.
    Diglyceride kinase from Escherichia coli. Purification in organic solvent and some properties of the enzyme (1979), Eur. J. Biochem., 94, 401-407.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
cardiolipin activates Escherichia coli
Lipid purified enzyme is completely inactive unless a lipid is added to the assay buffer containing Triton X-100 Escherichia coli
phosphatidylethanolamine plus cardiolipin, activates Escherichia coli
Span-20 activates Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
ceramide pH 6.6, 25°C Escherichia coli
1.4
-
ATP pH 6.6, 25°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
15000
-
1 * 15000, SDS-PAGE Escherichia coli
15400
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + ceramide
-
Escherichia coli ADP + ceramide 3-phosphate
-
?
additional information no activity with ficaprenol Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 15000, SDS-PAGE Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3 8.3
-
Escherichia coli

pI Value

Organism Comment pI Value Maximum pI Value
Escherichia coli isoelectric focusing
-
4