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Literature summary for 6.4.1.2 extracted from

  • Bettey, M.; Ireland, R.J.; Smith, A.M.
    Purification and characterization of acetyl CoA carboxylase from developing pea embryos (1992), J. Plant Physiol., 140, 513-520.
No PubMed abstract available
Search for more literature for 6.4.1.2

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Pisum sativum
CoA
-
 Pisum sativum
malonyl-CoA
-
 Pisum sativum
NADH
-
 Pisum sativum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
 acetyl-CoA mutant enzyme Pisum sativum
0.021
-
 acetyl-CoA wild type enzyme Pisum sativum
0.15
-
 acetyl-CoA MgATP2-, mutant enzyme Pisum sativum
0.16 0.19 ATP wild type enzyme Pisum sativum
2.8 3.5 HCO3- wild type Pisum sativum
3 3.5 HCO3- mutant enzyme Pisum sativum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
210000
-
 x * 210000, SDS-PAGE Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
 wild type BC1/7 RR and mutant BC1/7 rr
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pisum sativum

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
 Pisum sativum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.244
-
-
 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 + acetyl-CoA + hydrogencarbonate ATP in form of MgATP2- Pisum sativum ADP + phosphate + malonyl-CoA
-
 ?
ATP + butyryl-CoA + HCO3- 60% of the activity relative to acetyl-CoA Pisum sativum ADP + ethylmalonyl-CoA + phosphate
-
 ?

Subunits

Subunits Comment Organism
? x * 210000, SDS-PAGE Pisum sativum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.5
-
 Pisum sativum