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2.2.1.8 |
| Description |
Fluorothreonine transaldolase |
| Alternative names |
4-fluoro-L-threonine transaldolase;
fluoroacetaldehyde:L-threonine aldehydetransferase; |
| Catalyzed reaction |
L-threonine + fluoroacetaldehyde = acetaldehyde + 4-fluoro-L-threonine. |
| Cofactor |
Pyridoxal-phosphate. |
| Comments |
Can also convert chloroacetaldehyde into 4-chloro-L-threonine.
Unlike EC 2.1.2.1, glycine hydroxymethyltransferase, does not use glycine as a substrate. |
| Organisms |
-Eubacteria |
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Family |
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| Links |
Enzyme (activities) 2.2.1.8
BRENDA (activities) 2.2.1.8
KEGG (pathways) 2.2.1.8
PLPMDB (PLP mutants) 2.2.1.8
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| References |
Wu L, Tong MH, Raab A, Fang Q, Wang S, Kyeremeh K, Yu Y, Deng H
(2020) An unusual metal-bound 4-fluorothreonine transaldolase from Streptomyces sp. MA37 catalyses promiscuous transaldol reactions Appl Microbiol Biotechnol in press. Deng H, Cross SM, McGlinchey RP, Hamilton JT, O'Hagan D.
(2008) In vitro reconstituted biotransformation of 4-fluorothreonine from fluoride ion: application of the fluorinase Chem Biol 15 1268-76. Murphy, C.D.; 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 4479-4481. |
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| last changed |
2018/02/13 15:39 |
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