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Chemical Compound Review:

phosphothreonine (2S,3R)-2-amino-3- phosphonooxy-butanoic acid

Synonyms: AG-D-29930, AG-L-65882, CHEBI:37525, P1053_SIGMA, HMDB11185, ...

Brushaber, K.R. et al., Cheong, C.G. et al., Elia, A.E. et al.

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Disease relevance of phosphothreonine

CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2 [1].

High impact information on phosphothreonine

The three-dimensional structure of the pyridoxal 5'-phosphate (PLP)-dependent L-threonine-O-3-phosphate decarboxylase (CobD) from Salmonella enterica is described here [2].
Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates [3].

References

CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2. Brushaber, K.R., O'Toole, G.A., Escalante-Semerena, J.C. J. Biol. Chem. (1998) [Pubmed]
Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica. Cheong, C.G., Bauer, C.B., Brushaber, K.R., Escalante-Semerena, J.C., Rayment, I. Biochemistry (2002) [Pubmed]
Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates. Elia, A.E., Cantley, L.C., Yaffe, M.B. Science (2003) [Pubmed]

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