Fluorothreonine transaldolase

Fluorothreonine transaldolase (EC 2.2.1.8) is an enzyme that catalyzes the chemical reaction

Fluorothreonine transaldolase
Identifiers
EC no.2.2.1.8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins

The two substrates of the enzyme characterised from Streptomyces cattleya are L-threonine and fluoroacetaldehyde. Its products are 4-fluoro-L-threonine and acetaldehyde.[1][2]

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. It is pyridoxal phosphate dependent.[3]

References

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  1. 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". Angew. Chem. Int. Ed. Engl. 40 (23): 4479–4481. doi:10.1002/1521-3773(20011203)40:23<4479::AID-ANIE4479>3.0.CO;2-1. PMID 12404452.
  2. Murphy CD, Schaffrath C, O'Hagan D (2003). "Fluorinated natural products: the biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya". Chemosphere. 52 (2): 455–61. Bibcode:2003Chmsp..52..455M. doi:10.1016/S0045-6535(03)00191-7. PMID 12738270.
  3. Enzyme 2.2.1.8 at KEGG Pathway Database.