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Chemical Compound Review:

AG-K-62063 2-amino-3-oxo-butanoic acid

Synonyms: CHEMBL1160073, CHEBI:17844, ANW-64763, CTK5C2537, AR-1D8263, ...

Marcus, J.P. et al., Schmidt, A. et al., Mukherjee, J.J. et al.

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Disease relevance of alpha-amino-beta-ketobutyrate

Starting with 100 g (wet weight) of a mutant of Escherichia coli K-12 forced to grow on L-threonine as sole carbon source, we developed a 6-step procedure that provides 30-40 mg of homogeneous 2-amino-3-ketobutyrate CoA ligase (also called aminoacetone synthetase or synthase) [1].

High impact information on alpha-amino-beta-ketobutyrate

Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism [2].
Electron density maps indicated the presence in the crystal of the Schiff base intermediate of 2-amino-3-ketobutyrate and PLP, an external aldimine, which remained bound to KBL throughout the protein purification procedure [2].
pH-dependent decarboxylation of 2-amino-3-ketobutyrate, the unstable intermediate in the threonine dehydrogenase-initiated pathway for threonine utilization [3].

Analytical, diagnostic and therapeutic context of alpha-amino-beta-ketobutyrate

Using this system, we have found the half-life of 2-amino-3-ketobutyrate varies with pH from 8.6 minutes at pH 5.9 to 140 minutes at pH 11.1 yielding a theoretical titration curve that predicts a pKa value of 8.15 for the alpha-amino group of this intermediate [3].

References

Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme. Mukherjee, J.J., Dekker, E.E. J. Biol. Chem. (1987) [Pubmed]
Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism. Schmidt, A., Sivaraman, J., Li, Y., Larocque, R., Barbosa, J.A., Smith, C., Matte, A., Schrag, J.D., Cygler, M. Biochemistry (2001) [Pubmed]
pH-dependent decarboxylation of 2-amino-3-ketobutyrate, the unstable intermediate in the threonine dehydrogenase-initiated pathway for threonine utilization. Marcus, J.P., Dekker, E.E. Biochem. Biophys. Res. Commun. (1993) [Pubmed]

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