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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 |
-Eubacteria |
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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 |
Articles on 4.1.1.81 |
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last changed |
2019/06/19 09:10 |
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