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Chemical Compound Review:

ALLO-THREONINE (2S,3S)-2-amino-3-hydroxy- butanoic acid

Synonyms: Allo-Thr-OH, h-allo-thr-oh, AmbotzHAA1188, CHEMBL59238, AG-E-93850, ...

Kwon, Y.G. et al., Kwon, Y.G. et al., Liu, J.Q. et al., Liu, J.Q. et al., Liu, J.Q. et al., et al.

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Disease relevance of C05519

The predicted amino acid sequence displayed less than 20% identity with those of low-specificity L-TA from Saccharomyces cerevisiae, L-allo-threonine aldolase from Aeromonas jandaei, and four relevant hypothetical proteins from other microorganisms [1].
The ltaE gene encoding for a thermostable low-specificity L-threonine aldolase, which catalyzes the cleavage of L-threonine/L-allo-threonine to glycine and acetaldehyde, was cloned from Escherichia coli GS245 by the polymerase chain reaction [2].

High impact information on C05519

In an analogous vein, although beta-substituted alcohols that serve as PKA substrates must contain the same stereochemistry as that present in L-threonine, PKC will phosphorylate configurational isomers which correspond to both L-threonine and L-allo-threonine [3].
In an analogous vein, although beta-substituted alcohols that serve as PKA substrates must contain the same stereochemistry as that present in L-threonine, PKC will phosphorylate configurational isomers which correspond to both L-threonine and L-allo-threonine [4].
Proton nuclear magnetic resonance analysis of the enzyme reaction in deuterium oxide clearly showed epimerization from L- to D-allo-threonine and also from D- to L-allo-threonine [5].

Chemical compound and disease context of C05519

We have found that the GLY1 protein is similar in primary structure to L-allo-threonine aldolase of Aeromonas jandiae DK-39, which stereospecifically catalyzes the interconversion of L-allo-threonine and glycine [6].

References

Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558. Liu, J.Q., Ito, S., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S., Yamada, H. Appl. Environ. Microbiol. (1998) [Pubmed]
Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli. Liu, J.Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S., Yamada, H. Eur. J. Biochem. (1998) [Pubmed]
The active site substrate specificity of protein kinase C. Kwon, Y.G., Mendelow, M., Lawrence, D.S. J. Biol. Chem. (1994) [Pubmed]
The active site substrate specificity of protein kinase C. Kwon, Y.G., Mendelow, M., Lawrence, D.S. J. Biol. Chem. (1994) [Pubmed]
A new amino acid racemase with threonine alpha-epimerase activity from Pseudomonas putida: purification and characterization. Lim, Y.H., Yokoigawa, K., Esaki, N., Soda, K. J. Bacteriol. (1993) [Pubmed]
The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine--expression of the gene in Escherichia coli and purification and characterization of the enzyme. Liu, J.Q., Nagata, S., Dairi, T., Misono, H., Shimizu, S., Yamada, H. Eur. J. Biochem. (1997) [Pubmed]

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