Biology:Threonine-phosphate decarboxylase
From HandWiki
| 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 / QuickGO | ||||||||
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The enzyme threonine-phosphate decarboxylase (EC 4.1.1.81) catalyzes the chemical reaction
- L-threonine O-3-phosphate [math]\displaystyle{ \rightleftharpoons }[/math] (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
References
- "Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica". Biochemistry 41 (15): 4798–808. 2002. doi:10.1021/bi012111w. PMID 11939774.
- "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. 1995. doi:10.1074/jbc.270.40.23560. PMID 7559521.
- "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. 2002. 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. PMID 28137297.
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