Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.2 Thioester hydrolases
ID:3.1.2.29
Description:Fluoroacetyl-CoA thioesterase.
Cath: 3.10.129.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.2.29
BRENDA Enzyme Link: BRENDA 3.1.2.29
KEGG Enzyme Link: KEGG3.1.2.29
BioCyc Enzyme Link: BioCyc 3.1.2.29
ExPASy Enzyme Link: ExPASy3.1.2.29
EC2PDB Enzyme Link: EC2PDB 3.1.2.29
ExplorEnz Enzyme Link: ExplorEnz 3.1.2.29
PRIAM enzyme-specific profiles Link: PRIAM 3.1.2.29
IntEnz Enzyme Link: IntEnz 3.1.2.29
MEDLINE Enzyme Link: MEDLINE 3.1.2.29
MSA:

3.1.2.29;

Phylogenetic Tree:

3.1.2.29;

Uniprot:
M-CSA:
RHEA:28542 fluoroacetyl-CoA + H2O = CoA + fluoroacetate + H(+)
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[S;H0;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[SH;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural basis for the activity and substrate specificity of fluoroacetyl-CoA thioesterase FlK.Dias MV, Huang F, Chirgadze DY, Tosin M, Spiteller D, Dry EF, Leadlay PF, Spencer JB, Blundell TL2010 Jul 1620430898
The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: a thioesterase confers resistance to fluoroacetyl-coenzyme A.Huang F, Haydock SF, Spiteller D, Mironenko T, Li TL, O'Hagan D, Leadlay PF, Spencer JB2006 May16720268