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Literature summary extracted from

  • Mukherjee, J.J.; Dekker, E.E.
    Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme (1987), J. Biol. Chem., 262, 14441-14447.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.29 5,5'-dithiobis(2-nitrobenzoic acid)
-
Escherichia coli
2.3.1.29 iodoacetamide not Escherichia coli
2.3.1.29 N-ethylmaleimide
-
Escherichia coli
2.3.1.29 p-mercuribenzoate
-
Escherichia coli

General Stability

EC Number General Stability Organism
2.3.1.29 glycerol, 10% v/v, stabilizes Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.29 aminomalonic acid
-
Escherichia coli
2.3.1.29 Aminomethylphosphonic acid
-
Escherichia coli
2.3.1.29 Aminooxyacetate
-
Escherichia coli
2.3.1.29 Ba2+
-
Escherichia coli
2.3.1.29 Ca2+
-
Escherichia coli
2.3.1.29 Cd2+ strong Escherichia coli
2.3.1.29 CoA strong Escherichia coli
2.3.1.29 Cu2+ strong Escherichia coli
2.3.1.29 DTT
-
Escherichia coli
2.3.1.29 glutathione
-
Escherichia coli
2.3.1.29 Hg2+ strong Escherichia coli
2.3.1.29 hydroxylamine pyridoxal 5'-phosphate restores Escherichia coli
2.3.1.29 IAA
-
Escherichia coli
2.3.1.29 L-cysteine
-
Escherichia coli
2.3.1.29 Mn2+
-
Escherichia coli
2.3.1.29 additional information no inhibition by DTNB; not: PCMB, glycine methylester, glycinamide Escherichia coli
2.3.1.29 NaBH4
-
Escherichia coli
2.3.1.29 Ni2+
-
Escherichia coli
2.3.1.29 phenylhydrazine
-
Escherichia coli
2.3.1.29 Semicarbazide
-
Escherichia coli
2.3.1.29 Sr2+
-
Escherichia coli
2.3.1.29 Zn2+
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.29 0.059
-
acetyl-CoA
-
Escherichia coli
2.3.1.29 0.08
-
propionyl-CoA
-
Escherichia coli
2.3.1.29 12
-
butyryl-CoA
-
Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.29 41690
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition Escherichia coli
2.3.1.29 41930
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition Escherichia coli
2.3.1.29 42093
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition Escherichia coli
2.3.1.29 84190
-
calculated from amino acid composition Escherichia coli
2.3.1.29 85000
-
gel filtration Escherichia coli
2.3.1.29 90480
-
sucrose density gradient centrifugation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.29 acetyl-CoA + glycine Escherichia coli involved in L-threonine catabolism, inducible CoA + 2-amino-3-oxobutanoate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.29 Escherichia coli
-
K-12-mutant SBD-76, grown on L-threonine
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.1.29 additional information no carbohydrates Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.29
-
Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.29 2.76
-
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.29 acetyl-CoA + glycine not: valeryl-CoA, glutaryl-CoA Escherichia coli CoA + 2-amino-3-oxobutanoate
-
r
2.3.1.29 acetyl-CoA + glycine specific for glycine Escherichia coli CoA + 2-amino-3-oxobutanoate
-
r
2.3.1.29 acetyl-CoA + glycine succinyl-CoA Escherichia coli CoA + 2-amino-3-oxobutanoate
-
r
2.3.1.29 acetyl-CoA + glycine no substrate: L-alanine Escherichia coli CoA + 2-amino-3-oxobutanoate
-
r
2.3.1.29 acetyl-CoA + glycine no substrates: glycinamide, 2-aminoethanol, aminomethylphosphonic acid, aminomalonate Escherichia coli CoA + 2-amino-3-oxobutanoate
-
r
2.3.1.29 acetyl-CoA + glycine no substrate: glycine methylester Escherichia coli CoA + 2-amino-3-oxobutanoate
-
r
2.3.1.29 acetyl-CoA + glycine no substrates: L-serine, L-threonine, L-valine, L-leucine Escherichia coli CoA + 2-amino-3-oxobutanoate
-
r
2.3.1.29 acetyl-CoA + glycine involved in L-threonine catabolism, inducible Escherichia coli CoA + 2-amino-3-oxobutanoate
-
?
2.3.1.29 n-butyryl-CoA + glycine reaction at 16% the rate of acetyl-CoA Escherichia coli CoA + 2-amino-3-oxohexanoate
-
?
2.3.1.29 n-propionyl-CoA + glycine reaction at 127% the rate of acetyl-CoA Escherichia coli CoA + 2-amino-3-oxopentanoate
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.29 dimer 2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.29 25
-
assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.29 7.5
-
-
Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.1.29 6 9 about 30% of maximal activity at pH 6.0 and 43% at 9.0 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.29 pyridoxal 5'-phosphate
-
Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.1.29 0.14
-
aminomalonic acid
-
Escherichia coli
2.3.1.29 3.6
-
Aminomethylphosphonic acid
-
Escherichia coli