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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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pH-dependent decarboxylation of 2-amino-3-ketobutyrate, the unstable intermediate in the threonine dehydrogenase-initiated pathway for threonine utilization.

2-Amino-3-ketobutyrate can be readily formed enzymatically by the action of L-threonine dehydrogenase. A convenient assay for determining the half-life of this beta-keto acid is afforded by its rapid and quantitative conversion to glycine (+ acetyl CoA), as catalyzed by 2-amino-3-ketobutyrate CoA lyase. 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. These data are considered relevant to discussions pertaining to a threonine dehydrogenase/2-amino-3-ketobutyrate CoA lyase enzyme complex in the threonine utilization pathway and to mechanistic aspects of the 5-aminolevulinate synthase-catalyzed reaction where 2-amino-3-ketoadipate is involved.[1]

References

  1. 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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