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Literature summary extracted from

  • Yu, S.; Jensen, V.; Seeliger, J.; Feldmann, I.; Weber, S.; Schleicher, E.; Haeussler, S.; Blankenfeldt, W.
    Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein (2009), Biochemistry, 48, 10298-10307.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.2.32 structure of recombinant PqsE. The Protein possesses a metallo-beta-lactamase fold with an Fe(II)Fe(III) center in the active site. A copurified ligand is benzoate Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
3.1.2.32 E182A significant decrease in kcat value for S-(4-nitrobenzoyl)mercaptoethane Pseudomonas aeruginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.2.32 0.013
-
S-(4-nitrobenzoyl)mercaptoethane mutant E182A, pH 8.5, 25°C, presence of Mn2+ Pseudomonas aeruginosa
3.1.2.32 0.014
-
S-(4-nitrobenzoyl)mercaptoethane wild-type, pH 8.5, 25°C, presence of Mn2+ Pseudomonas aeruginosa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.2.32 Co2+ 9.7fold stimulation of EDTA-treated protein Pseudomonas aeruginosa
3.1.2.32 Fe2+ 3.3fold stimulation of EDTA-treated protein. Protein has a Fe(II)Fe(III) center in the active site, crystallization data Pseudomonas aeruginosa
3.1.2.32 Mn2+ 7.9fold stimulation of EDTA-treated protein Pseudomonas aeruginosa
3.1.2.32 Ni2+ 1.9fold stimulation of EDTA-treated protein Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.32 Pseudomonas aeruginosa P20581
-
-
3.1.2.32 Pseudomonas aeruginosa DSM 22644 P20581
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.32 2-aminobenzoylacetyl-CoA + H2O
-
Pseudomonas aeruginosa 2-aminobenzoylacetate + CoA
-
?
3.1.2.32 2-aminobenzoylacetyl-CoA + H2O
-
Pseudomonas aeruginosa DSM 22644 2-aminobenzoylacetate + CoA
-
?
3.1.2.32 additional information the enzyme slowly hydrolyzes phosphodiesters including single- and double-strandedDNA as well as mRNA and also the thioester S-(4-nitrobenzoyl)mercaptoethane. No substrates: acetyl-CoA, malonyl-CoA, benzoyl-CoA, L-lactoylglutathione Pseudomonas aeruginosa ?
-
?
3.1.2.32 additional information the enzyme slowly hydrolyzes phosphodiesters including single- and double-strandedDNA as well as mRNA and also the thioester S-(4-nitrobenzoyl)mercaptoethane. No substrates: acetyl-CoA, malonyl-CoA, benzoyl-CoA, L-lactoylglutathione Pseudomonas aeruginosa DSM 22644 ?
-
?
3.1.2.32 S-(4-nitrobenzoyl)mercaptoethane + H2O
-
Pseudomonas aeruginosa 4-nitrobenzoate + mercaptoethane
-
?
3.1.2.32 S-(4-nitrobenzoyl)mercaptoethane + H2O
-
Pseudomonas aeruginosa DSM 22644 4-nitrobenzoate + mercaptoethane
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.2.32 PA1000
-
Pseudomonas aeruginosa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.2.32 0.003
-
S-(4-nitrobenzoyl)mercaptoethane mutant E182A, pH 8.5, 25°C, presence of Mn2+ Pseudomonas aeruginosa
3.1.2.32 0.12
-
S-(4-nitrobenzoyl)mercaptoethane wild-type, pH 8.5, 25°C, presence of Mn2+ Pseudomonas aeruginosa