Threonine-phosphate decarboxylase

Last updated
threonine-phosphate decarboxylase
Identifiers
EC number 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

In enzymology, a threonine-phosphate decarboxylase (EC 4.1.1.81) is an enzyme that catalyzes the chemical reaction

L-threonine O-3-phosphate (R)-1-aminopropan-2-yl phosphate + CO2

Hence, this enzyme has one substrate, L-threonine O-3-phosphate, and two products, (R)-1-aminopropan-2-yl phosphate and CO2.

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.

See also

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References