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Literature summary for 2.3.1.29 extracted from

  • Mukherjee, J.J.; Dekker, E.E.
    2-Amino-3-ketobutyrate CoA ligase of Escherichia coli: stoichiometry of pyridoxal phosphate binding and location of the pyridoxyllysine peptide in the primary structure of the enzyme (1990), Biochim. Biophys. Acta, 1037, 24-29.
    View publication on PubMed

General Stability

General Stability Organism
EDTA, 1 mM, stabilizes Escherichia coli
ethylene glycol, 20%, stabilizes Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
84190
-
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + glycine
-
Escherichia coli CoA + 2-amino-3-oxobutanoate
-
?

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate requirement, stoichiometry: 1 mol per mol subunit Escherichia coli
pyridoxal 5'-phosphate location of pyridoxyllysine peptide in primary structure of enzyme Escherichia coli