Threonine-phosphate decarboxylase
In enzymology, a threonine-phosphate decarboxylase is an enzyme that catalyzes the chemical reaction
Hence, this enzyme has one substrate, L-threonine O-3-phosphate, and two products, -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 . 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 in anaerobic bacteria such as Salmonella typhimurium and Bacillus megaterium. In the next step, -1-aminopropan-2-ol is attached to adenosylcobyric acid, forming adenosylcobinamide phosphate.
