Threonine-phosphate decarboxylase

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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 $\rightleftharpoons$ (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.

[edit] References

IUBMB entry for 4.1.1.81
BRENDA references for 4.1.1.81 (Recommended.)
PubMed references for 4.1.1.81
PubMed Central references for 4.1.1.81
Google Scholar references for 4.1.1.81
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: 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: 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: 390–412. doi:10.1039/b108967f. PMID 12195810.