Threonine-phosphate decarboxylase
threonine-phosphate decarboxylase | |||||||||
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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 / EGO | ||||||||
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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 participates in porphyrin and chlorophyll metabolism.
References
- Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I (2002). "Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica". Biochemistry. 41 (15): 4798–808. doi:10.1021/bi012111w. PMID 11939774.
- O'Toole GA, Escalante-Semerena JC (1995). "Purification and characterization of the bifunctional CobU enzyme of Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate". J. Biol. Chem. 270 (40): 23560–9. doi:10.1074/jbc.270.40.23560. PMID 7559521.
- Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. doi:10.1039/b108967f. PMID 12195810.
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