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Literature summary for 2.3.3.8 extracted from

  • Guy, P.S.; Cohen, P.; Hardie, D.G.
    Purification and physicochemical properties of ATP citrate (pro-3S) lyase from lactating rat mammary gland and studies of its reversible phosphorylation (1981), Eur. J. Biochem., 114, 399-405.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
CoA phosphorylated enzyme Rattus norvegicus
0.18
-
citrate phosphorylated enzyme Rattus norvegicus
0.57
-
ATP phosphorylated enzyme Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
116000
-
4 * 116000, SDS-PAGE Rattus norvegicus
473000
-
equilibrium sedimentation Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification phosphoprotein Rattus norvegicus
side-chain modification contains 2 mol phosphate per mol of tetramer Rattus norvegicus
side-chain modification regulation of the enzyme by reversible phosphorylation. The enzyme which has been phosphorylated by cyclic-AMP-dependent protein kinase, can be completely dephosphorylated by incubation with either protein phosphatase 1 or protein phosphatase 2 Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
mammary gland Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
mammary gland lactating Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Rattus norvegicus

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer 4 * 116000, SDS-PAGE Rattus norvegicus