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4.1.1.81 |
| Description |
Threonine-phosphate decarboxylase. |
| Alternative names |
L-threonine-O-3-phosphate decarboxylase;
CobD |
| Catalyzed reaction |
L-threonine O-3-phosphate = (R)-1-aminopropan-2-ol phosphate + CO(2). |
| Cofactor |
Pyridoxal-phosphate |
| Comments |
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. |
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In Salmonella enterica, this enzyme is coded by the CobD gene, and its role in cobalamin biosynthesis has been established. Structurally the Salmonella protein shows a strong similarity to histidinol phosphate aminotransferase (2.6.1.9) |
| PDB |
1LKC; |
| Organisms |
-Bacteria |
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Family |
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| Links |
Enzyme (activities) 4.1.1.81
BRENDA (activities) 4.1.1.81
KEGG (pathways) 4.1.1.81
PLPMDB (PLP mutants) 4.1.1.81
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| References |
Santos F, Vera JL, van der Heijden R, Valdez G, de Vos WM, Sesma F, Hugenholtz J. (2008) The complete coenzyme B12 biosynthesis gene cluster of Lactobacillus reuteri CRL1098 Microbiology 154 81-93. Cheong, C.G.; Bauer, C.B.; Brushaber, K.R.; Escalante-Semerena, J.C.; Rayment, I. (2002) Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica Biochemistry 41 4798-808. Brushaber, K.R.; O'Toole, G.A.;Escalante-Semerena, J.C. (1998) 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 2684-91. . |
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| last changed |
2008/01/30 17:40 |
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