Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Sumper, M.
    Acetyl-CoA carboxylase from yeast (1981), Methods Enzymol., 71, 34-37.
    View publication on PubMed

General Stability

EC Number General Stability Organism
6.4.1.2 low ionic strength and alkaline pH favor the rapid inactivation of the enzyme Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.4.1.2 189000
-
 4 * 189000, SDS-PAGE Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
6.4.1.2 Saccharomyces cerevisiae
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.4.1.2 6
-
-
 Saccharomyces cerevisiae

Storage Stability

EC Number Storage Stability Organism
6.4.1.2 -20°C, 0.3 M potassium phosphate, 50% glycerol, pH 6.5, stable for at least 1 year Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.4.1.2 ATP + acetyl-CoA + HCO3-
-
 Saccharomyces cerevisiae ADP + phosphate + malonyl-CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
6.4.1.2 tetramer 4 * 189000, SDS-PAGE Saccharomyces cerevisiae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
6.4.1.2 8
-
 rapid inactivation above. Dissociation of the tetrameric native enzyme in a mixture of monomers, dimers and trimers Saccharomyces cerevisiae