Threonine-phosphate decarboxylase
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The enzyme threonine-phosphate decarboxylase (EC 4.1.1.81) catalyzes the chemical reaction
- L-threonine O-3-phosphate (R)-1-aminopropan-2-yl phosphate + CO2
Quick Facts Identifiers, EC no. ...
threonine-phosphate decarboxylase | |||||||||
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Identifiers | |||||||||
EC no. | 4.1.1.81 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-threonine-O-3-phosphate carboxy-lyase [(R)-1-aminopropan-2-yl-phosphate-forming]. Other names in common use include L-threonine-O-3-phosphate decarboxylase, CobD and L-threonine-O-3-phosphate carboxy-lyase. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria such as Salmonella typhimurium and Bacillus megaterium. In the next step, (R)-1-aminopropan-2-ol is attached to adenosylcobyric acid, forming adenosylcobinamide phosphate.