Threonine-phosphate decarboxylase

The enzyme threonine-phosphate decarboxylase (EC 4.1.1.81) catalyzes the chemical reaction

L-threonine O-3-phosphate ${\displaystyle \rightleftharpoons }$ (R)-1-aminopropan-2-yl phosphate + 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

• Cobalamin biosynthesis

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. CiteSeerX 10.1.1.564.9386. 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.
• Fang, H; Kang, J; Zhang, D (30 January 2017). "Microbial production of vitamin B₁₂: a review and future perspectives". Microbial Cell Factories. 16 (1): 15. doi:10.1186/s12934-017-0631-y. PMC 5282855. PMID 28137297.

This page was last edited on 1 December 2023, at 02:45