Enzyme

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EC Tree
     2. Transferases
        2.2 Transferring aldehyde or ketonic groups
            2.2.1 Transketolases and transaldolases
ID:2.2.1.8
Description:Fluorothreonine transaldolase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.2.1.8
BRENDA Enzyme Link: BRENDA 2.2.1.8
KEGG Enzyme Link: KEGG2.2.1.8
BioCyc Enzyme Link: BioCyc 2.2.1.8
ExPASy Enzyme Link: ExPASy2.2.1.8
EC2PDB Enzyme Link: EC2PDB 2.2.1.8
ExplorEnz Enzyme Link: ExplorEnz 2.2.1.8
PRIAM enzyme-specific profiles Link: PRIAM 2.2.1.8
IntEnz Enzyme Link: IntEnz 2.2.1.8
MEDLINE Enzyme Link: MEDLINE 2.2.1.8
MSA:

2.2.1.8;

Phylogenetic Tree:

2.2.1.8;

Uniprot:
M-CSA:
RHEA:11748 fluoroacetaldehyde + L-threonine = 4-fluoro-L-threonine + acetaldehyde
RULE(radius=1) [*:1]-[CH2;+0:2]-[F;H0;+0:3].[*:4]-[CH3;+0:5]>>[*:4]-[CH2;+0:5]-[F;H0;+0:3].[*:1]-[CH3;+0:2]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
In vitro reconstituted biotransformation of 4-fluorothreonine from fluoride ion: application of the fluorinase.Deng H, Cross SM, McGlinchey RP, Hamilton JT, O'Hagan D2008 Dec 2219101471
Fluorinated natural products: the biosynthesis of fluoroacetate and 4-fluorothreonine in Streptomyces cattleya.Murphy CD, Schaffrath C, O'Hagan D2003 Jul12738270
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. Murphy CD, O'Hagan D, Schaffrath C2001 Dec 312404452