The Enzyme Database

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Accepted name: threonine-phosphate decarboxylase
Reaction: L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO2
For diagram of corrin biosynthesis (part 6), click here
Other name(s): L-threonine-O-3-phosphate decarboxylase; CobD; L-threonine-O-3-phosphate carboxy-lyase
Systematic name: L-threonine-O-3-phosphate carboxy-lyase [(R)-1-aminopropan-2-yl-phosphate-forming]
Comments: 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, adenosylcobinamide-phosphate synthase, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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 (2002) 4798–4808. [DOI] [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 (1998) 2684–2691. [DOI] [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 (2002) 390–412. [PMID: 12195810]
[EC created 2004]

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