EC - Threonine-phosphate decarboxylase

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IntEnz Enzyme Nomenclature


Accepted name:
threonine-phosphate decarboxylase
Other names:
L-threonine-O-3-phosphate decarboxylase
L-threonine O-3-phosphate carboxy-lyase
Systematic name:
L-threonine-O-3-phosphate carboxy-lyase [(R)-1-aminopropan-2-yl-phosphate-forming]




A pyridoxal-phosphate protein. This enzyme is unable to decarboxylate the D-isomer of threonine O-3-phosphate. The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC, 5'-deoxyadenosylcobinamide phosphate synthase, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0048472


  1. Cheong, C.G., Bauer, C.B., Brushaber, K.R., Escalante-Semerena, J.C. and Rayment, I.
    Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica.
    Biochemistry 41: 4798-4808 (2002). [PMID: 11939774]
  2. Brushaber, K.R., O'Toole, G.A. and Escalante-Semerena, J.C.
    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.
    J. Biol. Chem. 273: 2684-2691 (1998). [PMID: 9446573]
  3. Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C.
    The biosynthesis of adenosylcobalamin (vitamin B12).
    Nat. Prod. Rep. 19: 390-412 (2002). [PMID: 12195810]

[EC created 2004]