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Literature summary for 2.3.1.29 extracted from

  • Mukherjee, J.J.; Dekker, E.E.
    Inactivation of Escherichia coli 2-amino-3-ketobutyrate CoA ligase by phenylglyoxal and identification of an active-site arginine peptide (1992), Arch. Biochem. Biophys., 299, 147-153.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
1,2-Cyclohexanedione inactivation Escherichia coli
2,3-Butanedione inactivation Escherichia coli
4-(Oxoacetyl)phenoxyacetic acid
-
 Escherichia coli
Phenylglyoxal inactivation, 50% protection by pyridoxal 5'-phosphate or CoA (glycine or threonine to some extent), kinetics Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
12
-
 glycine
-
 Escherichia coli

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification the phenylglyoxal-inactivated enzyme is associated with the loss of 1.5 arginine residue per ligase subunit Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate active-site mapping Escherichia coli