EC |
4.1.1.81 |
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 6.3.1.10, adenosylcobinamide-phosphate synthase, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
References: |
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 4.1.1.81 created 2004] |
|
|
|
|