Biology:Fluorothreonine transaldolase
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Short description: Enzyme
| Fluorothreonine transaldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.2.1.8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a fluorothreonine transaldolase (EC 2.2.1.8) is an enzyme that catalyzes the chemical reaction
- L-threonine + fluoroacetaldehyde [math]\displaystyle{ \rightleftharpoons }[/math] acetaldehyde + 4-fluoro-L-threonine
Thus, the two substrates of this enzyme are L-threonine and fluoroacetaldehyde, whereas its two products are acetaldehyde and 4-fluoro-L-threonine.
This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name of this enzyme class is fluoroacetaldehyde:L-threonine aldehydetransferase.
References
- "Identification of a PLP-Dependent Threonine Transaldolase: A Novel Enzyme Involved in 4-Fluorothreonine Biosynthesis in Streptomyces cattleya This work was supported by the Biotechnological and Biological Sciences Research Council and the University of St Andrews". Angew. Chem. Int. Ed. Engl. 40 (23): 4479–4481. 2001. doi:10.1002/1521-3773(20011203)40:23<4479::AID-ANIE4479>3.0.CO;2-1. PMID 12404452.
- "Fluorinated natural products: the biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya". Chemosphere 52 (2): 455–61. 2003. doi:10.1016/S0045-6535(03)00191-7. PMID 12738270.
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