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Literature summary for 2.3.3.8 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

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

Cloned(Commentary)

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

Purification (Comment) Organism
recombinant enzyme Homo sapiens

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

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