Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.2 Thioester hydrolases
ID:3.1.2.32
Description:2-aminobenzoylacetyl-CoA thioesterase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.2.32
BRENDA Enzyme Link: BRENDA 3.1.2.32
KEGG Enzyme Link: KEGG3.1.2.32
BioCyc Enzyme Link: BioCyc 3.1.2.32
ExPASy Enzyme Link: ExPASy3.1.2.32
EC2PDB Enzyme Link: EC2PDB 3.1.2.32
ExplorEnz Enzyme Link: ExplorEnz 3.1.2.32
PRIAM enzyme-specific profiles Link: PRIAM 3.1.2.32
IntEnz Enzyme Link: IntEnz 3.1.2.32
MEDLINE Enzyme Link: MEDLINE 3.1.2.32
MSA:

3.1.2.32;

Phylogenetic Tree:

3.1.2.32;

Uniprot:
M-CSA:
RHEA:49444 (2-aminobenzoyl)acetyl-CoA + H2O = (2-aminobenzoyl)acetate + CoA + 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
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References

TitleAuthorsDatePubMed ID
PqsE of Pseudomonas aeruginosa Acts as Pathway-Specific Thioesterase in the Biosynthesis of Alkylquinolone Signaling Molecules.Drees SL, Fetzner S2015 May 2125960261
Dissecting the Multiple Roles of PqsE in Pseudomonas aeruginosa Virulence by Discovery of Small Tool Compounds.Zender M, Witzgall F, Drees SL, Weidel E, Maurer CK, Fetzner S, Blankenfeldt W, Empting M, Hartmann RW2016 Jun 1727082157
Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein.Yu S, Jensen V, Seeliger J, Feldmann I, Weber S, Schleicher E, Häussler S, Blankenfeldt W2009 Nov 319788310