Fluorothreonine transaldolase

From Wikipedia, the free encyclopedia

In enzymology, a fluorothreonine transaldolase (EC 2.2.1.8) is an enzyme that catalyzes the chemical reaction

L-threonine + fluoroacetaldehyde 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.

[edit] References

• IUBMB entry for 2.2.1.8
• BRENDA references for 2.2.1.8 (Recommended.)
• PubMed references for 2.2.1.8
• PubMed Central references for 2.2.1.8
• Google Scholar references for 2.2.1.8
• Murphy CD, O'Hagan D, Schaffrath C (2001). "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: 4479–4481. doi:10.1002/1521-3773(20011203)40:23<4479::AID-ANIE4479>3.0.CO;2-1. PMID 12404452. 
• Murphy CD, Schaffrath C, O'Hagan D (2003). "Fluorinated natural products: the biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya". Chemosphere. 52: 455–61. doi:10.1016/S0045-6535(03)00191-7. PMID 12738270. 

[edit] External links

• IUBMB entry for 2.2.1.8

• KEGG entry for 2.2.1.8

• BRENDA entry for 2.2.1.8

• NiceZyme view of 2.2.1.8

• EC2PDB: PDB structures for 2.2.1.8

• PRIAM entry for 2.2.1.8

• PUMA2 entry for 2.2.1.8

• IntEnz: Integrated Enzyme entry for 2.2.1.8

• MetaCyc entry for 2.2.1.8

• Atomic-resolution structures of enzymes belonging to this class