L-threonine kinase
| L-threonine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.177 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
L-threonine kinase (EC 2.7.1.177, PduX) is an enzyme with systematic name ATP:L-threonine O3-phosphotransferase. This enzyme catalyses the following chemical reaction
The enzyme characterised from the bacterium, Salmonella enterica, converts the amino acid, L-threonine, to threonine phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The reaction is part of the biosynthesis of adenosylcobalamin in this organism.[1][2]
The enzyme takes part in the synthesis of adenosylcobalamin.
References
- ↑ Fan C, Bobik TA (April 2008). "The PduX enzyme of Salmonella enterica is an L-threonine kinase used for coenzyme B12 synthesis". The Journal of Biological Chemistry. 283 (17): 11322–9. doi:10.1074/jbc.m800287200. PMID 18308727.
- ↑ Fan C, Fromm HJ, Bobik TA (July 2009). "Kinetic and functional analysis of L-threonine kinase, the PduX enzyme of Salmonella enterica". The Journal of Biological Chemistry. 284 (30): 20240–8. doi:10.1074/jbc.m109.027425. PMC 2740450. PMID 19509296.
External links
- L-threonine+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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