Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.97 extracted from

  • Bokhove, M.; Nadal Jimenez, P.; Quax, W.J.; Dijkstra, B.W.
    The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket (2010), Proc. Natl. Acad. Sci. USA, 107, 686-691.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cloned and overexpressed Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment) Organism
1.8 A resolution. PvdQ has a typical alpha/beta heterodimeric Ntn-hydrolase fold. It has a large, hydrophobic binding pocket, ideally suited to recognize C12 fatty acid-like chains of N-acylhomoserine lactones. Binding of a C12 fatty acid or a 3-oxo-C12 fatty acid induces subtle conformational changes to accommodate the aliphatic chain. PvdQ is the first structurally characterized Ntn-hydrolase within this family to have any disulfide bridges. The disulfides are located in both the alpha- and beta-chain on the periphery of the protein Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9I194
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-3-oxodecanoyl-L-homoserine lactone + H2O
-
Pseudomonas aeruginosa L-homoserine lactone + 3-oxodecanoic acid
-
?

Synonyms

Synonyms Comment Organism
AHL acylase
-
Pseudomonas aeruginosa
PvdQ
-
Pseudomonas aeruginosa
quorum-quenching N-acyl homoserine lactone acylase PvdQ
-
Pseudomonas aeruginosa