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Literature summary extracted from

  • Potapova, I.A.; El-Maghrabi, M.R.; Doronin, S.V.; Benjamin, W.B.
    Phosphorylation of recombinant human ATP:citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. Allosteric activation of ATP:citrate lyase by phosphorylated sugars (2000), Biochemistry, 39, 1169-1179.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.3.8 D-fructose 1,6-diphosphate activates Homo sapiens
2.3.3.8 D-fructose 2,6-diphosphate activates Homo sapiens
2.3.3.8 D-fructose 6-phosphate potent activator of the unphosphorylated recombinant enzyme, half-maximal activation at 0.16 mM Homo sapiens
2.3.3.8 D-glucose 1-phosphate activates Homo sapiens
2.3.3.8 D-glucose 6-phosphate activates Homo sapiens
2.3.3.8 D-ribulose 5-phosphate activates Homo sapiens
2.3.3.8 D-xylulose 5-phosphate activates Homo sapiens
2.3.3.8 phosphoenolpyruvate activates Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.3.8 expression in Escherichia coli Homo sapiens
2.3.3.8 expression in Escherichia coli Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.3.8 additional information
-
 additional information
-
 Rattus norvegicus
2.3.3.8 additional information
-
 additional information Km-value for phosphorylated enzyme forms Homo sapiens
2.3.3.8 2.59
-
 CoA
-
 Homo sapiens
2.3.3.8 41
-
 ATP
-
 Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.3.8 120000
-
 x * 120000, SDS-PAGE Homo sapiens
2.3.3.8 480000
-
 velocity sedimentation Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.8 Homo sapiens
-
-
-
2.3.3.8 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.3.8 phosphoprotein phosphorylation of recombinant human ATP:citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. Cyclic AMP-dependent protein kinase catalyzes the incorporation of 1 mol of phosphate per mol of enzyme homotetramer, and glycogen synthase kinase-3 incorporated an additional 2 mol of phosphate into the phosphorylated protein Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.3.8 recombinant enzyme Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.3.8 2
-
 recombinant enzyme Homo sapiens

Storage Stability

EC Number Storage Stability Organism
2.3.3.8 -20°C, 1 year, stable Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.3.8 ATP + citrate + CoA
-
 Homo sapiens ADP + phosphate + acetyl-CoA + oxaloacetate
-
 ?
2.3.3.8 ATP + citrate + CoA
-
 Rattus norvegicus ADP + phosphate + acetyl-CoA + oxaloacetate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.3.8 ?
-
 Rattus norvegicus
2.3.3.8 ? x * 120000, SDS-PAGE Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.3.8 30
-
 4 h, stable Homo sapiens