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

BRENDA support

Literature summary for 2.3.1.29 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

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

General Stability

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

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information no carbohydrates Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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

pH Optimum

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

pH Range

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Escherichia coli

Ki Value [mM]

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