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Literature summary for 6.4.1.2 extracted from

  • Dehaye, L.; Alban, C.; Job, C.; Douce, R.; Job, D.
    Kinetics of the two forms of acetyl-CoA carboxylase from Pisum sativum. Correlation of the substrate specificity of the enzymes and sensitivity towards aryloxyphenoxypropionate herbicides (1994), Eur. J. Biochem., 225, 1113-1123.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
Quizalofop seed enzyme which carboxylates acety-CoA and propionyl-CoA has two separate active sites. One site binds either acetyl-CoA or propionyl-CoA and is inhibited by quizalofop. The other site is specific for acetyl-CoA and is much less inhibited by quizalofop. The leaf enzyme is not able to carboxylate propionyl-CoA and is insensitive to quizalofop Pisum sativum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.038
-
 ATP propionyl-CoA Pisum sativum
0.226
-
 acetyl-CoA
-
 Pisum sativum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
220000
-
 2 * 220000, SDS-PAGE Pisum sativum
480000
-
 seed enzyme, gel filtration Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pisum sativum

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
 Pisum sativum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.092
-
 seed Pisum sativum
0.121
-
 leaf Pisum sativum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetyl-CoA + HCO3-
-
 Pisum sativum ADP + phosphate + malonyl-CoA
-
 ?
ATP + propionyl-CoA + HCO3- maximal rate is 20% of that for acetyl-CoA Pisum sativum ADP + phosphate + methylmalonyl-CoA
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 220000, SDS-PAGE Pisum sativum