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Literature summary for 3.5.1.97 extracted from

  • Liu, N.; Yu, M.; Zhao, Y.; Cheng, J.; An, K.; Zhang, X.H.
    PfmA, a novel quorum-quenching N-acylhomoserine lactone acylase from Pseudoalteromonas flavipulchra (2017), Microbiology, 163, 1389-1398 .
    View publication on PubMed
Search for more literature for 3.5.1.97

Cloned(Commentary)

Cloned (Comment) Organism
gene pfmA, sequence comparisons, cloning of PfmA and recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Pseudoalteromonas flavipulchra

Protein Variants

Protein Variants Comment Organism
H278S site-directed mutagenesis, the mutant shows 80% reduced activity compared to wild-type Pseudoalteromonas flavipulchra
L279S site-directed mutagenesis, the mutant shows 74% reduced activity compared to wild-type Pseudoalteromonas flavipulchra

Inhibitors

Inhibitors Comment Organism Structure
Mn2+ about 10% inhibition at 1 mM Pseudoalteromonas flavipulchra
Ni2+ about 10% inhibition at 1 mM Pseudoalteromonas flavipulchra
SDS complete inhibition at 1 mM Pseudoalteromonas flavipulchra
Urea 20% inhibition at 1 mM Pseudoalteromonas flavipulchra
Zn2+ about 10% inhibition at 1 mM Pseudoalteromonas flavipulchra

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular PfmA lacks an N-terminal signal peptide and no activity is found in the cell medium Pseudoalteromonas flavipulchra 5622
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ increases the enzyme activity by 8.5% at 1 mM Pseudoalteromonas flavipulchra
additional information Na+, K+, Ca2+, Fe3+, and Cu2+ show no or poor effects on AHL acylase activity at 1 mM Pseudoalteromonas flavipulchra

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
91000
-
 about, sequence calculation Pseudoalteromonas flavipulchra

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudoalteromonas flavipulchra the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present ?
-
-
additional information Pseudoalteromonas flavipulchra JG1 the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present ?
-
-
N-3-oxo-decanoyl-L-homoserine lactone + H2O Pseudoalteromonas flavipulchra
-
 L-homoserine lactone + 3-oxodecanoate
-
 ?
N-3-oxo-dodecanoyl-L-homoserine lactone + H2O Pseudoalteromonas flavipulchra
-
 L-homoserine lactone + 3-oxododecanoate
-
 ?
N-3-oxo-tetradecanoyl-L-homoserine lactone + H2O Pseudoalteromonas flavipulchra
-
 L-homoserine lactone + 3-oxotetradecanoate
-
 ?
N-decanoyl-L-homoserine lactone + H2O Pseudoalteromonas flavipulchra
-
 L-homoserine lactone + decanoate
-
 ?
N-decanoyl-L-homoserine lactone + H2O Pseudoalteromonas flavipulchra JG1
-
 L-homoserine lactone + decanoate
-
 ?
N-dodecanoyl-L-homoserine lactone + H2O Pseudoalteromonas flavipulchra
-
 L-homoserine lactone + dodecanoate
-
 ?
N-dodecanoyl-L-homoserine lactone + H2O Pseudoalteromonas flavipulchra JG1
-
 L-homoserine lactone + dodecanoate
-
 ?
N-tetradecanoyl-L-homoserine lactone + H2O Pseudoalteromonas flavipulchra
-
 L-homoserine lactone + tetradecanoate
-
 ?
N-tetradecanoyl-L-homoserine lactone + H2O Pseudoalteromonas flavipulchra JG1
-
 L-homoserine lactone + tetradecanoate
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudoalteromonas flavipulchra A0A223AMX9
-
-
Pseudoalteromonas flavipulchra JG1 A0A223AMX9
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification post-translational modification is performed prior to PfmA becoming an active enzyme Pseudoalteromonas flavipulchra

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Pseudoalteromonas flavipulchra

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present Pseudoalteromonas flavipulchra ?
-
-
additional information enzyme AHL acylase PfmA can degrade N-acylhomoserine lactones (AHLs) with acyl chains longer than 10 carbons. PfmA can degrade ampicillin but not penicillin G. No activity with N-hexanoyl-L-homoserine lactone, N-3-oxo-hexanoyl-L-homoserine lactone, N-octanoyl-L-homoserine lactone, and N-3-oxo-octanoyl-L-homoserine lactone Pseudoalteromonas flavipulchra ?
-
-
additional information the marine bacterium Pseudoalteromonas flavipulchra strain JG1 can degrade N-acylhomoserine lactones (AHLs). PfmA can degrade ampicillin but not penicillin G. The concentration of AHLs in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1 is reduced when 0.01 mg/ml PfmA is present Pseudoalteromonas flavipulchra JG1 ?
-
-
additional information enzyme AHL acylase PfmA can degrade N-acylhomoserine lactones (AHLs) with acyl chains longer than 10 carbons. PfmA can degrade ampicillin but not penicillin G. No activity with N-hexanoyl-L-homoserine lactone, N-3-oxo-hexanoyl-L-homoserine lactone, N-octanoyl-L-homoserine lactone, and N-3-oxo-octanoyl-L-homoserine lactone Pseudoalteromonas flavipulchra JG1 ?
-
-
N-3-oxo-decanoyl-L-homoserine lactone + H2O
-
 Pseudoalteromonas flavipulchra L-homoserine lactone + 3-oxodecanoate
-
 ?
N-3-oxo-dodecanoyl-L-homoserine lactone + H2O
-
 Pseudoalteromonas flavipulchra L-homoserine lactone + 3-oxododecanoate
-
 ?
N-3-oxo-tetradecanoyl-L-homoserine lactone + H2O
-
 Pseudoalteromonas flavipulchra L-homoserine lactone + 3-oxotetradecanoate
-
 ?
N-decanoyl-L-homoserine lactone + H2O
-
 Pseudoalteromonas flavipulchra L-homoserine lactone + decanoate
-
 ?
N-decanoyl-L-homoserine lactone + H2O
-
 Pseudoalteromonas flavipulchra JG1 L-homoserine lactone + decanoate
-
 ?
N-dodecanoyl-L-homoserine lactone + H2O
-
 Pseudoalteromonas flavipulchra L-homoserine lactone + dodecanoate
-
 ?
N-dodecanoyl-L-homoserine lactone + H2O
-
 Pseudoalteromonas flavipulchra JG1 L-homoserine lactone + dodecanoate
-
 ?
N-tetradecanoyl-L-homoserine lactone + H2O
-
 Pseudoalteromonas flavipulchra L-homoserine lactone + tetradecanoate
-
 ?
N-tetradecanoyl-L-homoserine lactone + H2O
-
 Pseudoalteromonas flavipulchra JG1 L-homoserine lactone + tetradecanoate
-
 ?

Subunits

Subunits Comment Organism
heterodimer 1 * 26000, alpha-subunit, + 1 * 68000, beta-subunit, His6-tagged recombinant enzyme, SDS-PAGE Pseudoalteromonas flavipulchra
More second-structure analysis of PfmA shows that the protein includes an alpha subunit, a spacer sequence, and a beta subunit. The alpha subunit of PfmA is predicted to have seven alpha helices, two beta folds and three random coils, while the beta subunit is predicted to have 12 alpha helices, 19 beta folds and eight random coils Pseudoalteromonas flavipulchra

Synonyms

Synonyms Comment Organism
FaGL1422
-
 Pseudoalteromonas flavipulchra
N-acylhomoserine lactone acylase
-
 Pseudoalteromonas flavipulchra
pfmA
-
 Pseudoalteromonas flavipulchra
quorum-quenching N-acylhomoserine lactone acylase
-
 Pseudoalteromonas flavipulchra

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Pseudoalteromonas flavipulchra

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 80 over 40% of maximal activity at 20-80°C, profile overview Pseudoalteromonas flavipulchra

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 30 purified recombinant enzyme, completely stable at Pseudoalteromonas flavipulchra
40
-
 purified recombinant enzyme, 40% activity remaining Pseudoalteromonas flavipulchra
50
-
 purified recombinant enzyme, 30% activity remaining Pseudoalteromonas flavipulchra
60
-
 purified recombinant enzyme, 10% activity remaining Pseudoalteromonas flavipulchra
70
-
 purified recombinant enzyme, 5% activity remaining Pseudoalteromonas flavipulchra
80
-
 purified recombinant enzyme, no activity remaining Pseudoalteromonas flavipulchra

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Pseudoalteromonas flavipulchra

pH Range

pH Minimum pH Maximum Comment Organism
4 11 over 50% of maximal activity at pH 5.0-11.0, 40% at pH 4.0, profile overview Pseudoalteromonas flavipulchra

General Information

General Information Comment Organism
evolution enzyme PfmA belongs to the N-terminal nucleophile (Ntn) hydrolase superfamily and shows homology to a member of penicillin amidases, but PfmA can degrade ampicillin but not penicillin G Pseudoalteromonas flavipulchra
additional information residue Ser256 in PfmA is the active site residue and residues Arg528, Asn324, His278 and Leu279 also play important roles in the catalytic process. Ser356 is also the first amino acid of the beta-subunit Pseudoalteromonas flavipulchra
physiological function enzyme PfmA reduces N-acylhomoserine lactone (AHL) accumulation and the production of virulence factors in Vibrio anguillarum strain VIB72 and Pseudomonas aeruginosa strain PAO1, and attenuates the virulence of Pseudomonas aeruginosa to increase Artemia survival, which suggests that PfmA can be considered as a therapeutic agent to control AHL-mediated pathogenicity. N-acylhomoserine lactone acylase is a quorum-quenching enzyme. Quorum sensing (QS) is a cell-to-cell communication mechanism dependent on cell density, which allows bacterial populations to regulate the expression of genes responsible for a wide range of biological behaviours, such as the production of pigments, biofilm formation, antibiotic production, motility, adhesion, bioluminescence and secretion of virulence factors Pseudoalteromonas flavipulchra