EC Number   |
General Information |
Reference |
|---|
   3.5.1.97 | 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 |
-, 757621 |
| 3.5.1.97 | evolution |
the acylase gene APTM01 from the strain MQS005 belongs to PvdQ type on sub-branch in phylogenetic tree |
-, 756541 |
| 3.5.1.97 | evolution |
the enzyme belongs to the amidase family. AmiE shows homology with a member of the amidases (EC 3.5.1.4) but not with any known AHL acylase enzymes. An amino acid sequence of AmiE from Ooi24 shows greater than 99% identities with uncharacterized proteins from Acinetobacter ursingii CIP 107286 and Acinetobacter sp. strain CIP 102129, but it is not found in the draft or complete genome sequences of other Acinetobacter strains. Phylogenetic relationship between AmiE and known AHL acylases and phylogenetic tree |
731186 |
| 3.5.1.97 | evolution |
the enzyme shows an AHL acylase type mode of action. It possesses similarity with an alpha/beta-hydrolase fold protein, which makes it unique among the known AHL acylases with domains of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Phylogenetic analysis of isolate VM4 within the genus Delftia |
758124 |
| 3.5.1.97 | metabolism |
virulence gene expression in many Gram-negative pathogens generally is under quorum sensing control. In particular, quorum-sensing plays an important role in the regulation of virulence genes (mainly plant cell wall degrading enzymes, PCWDEs, production) in phytopathogenic soft rot causing Pectobacterium species. Also the N-acylhomoserine lactone (AHL) based quorum sensing in soft rot Pectobacterium species tightly regulates the activities implicated in microbial competition and host-pathogen interaction. These activities require various microbial functions such as biofilm formation, expression of virulence factors, antibiotic production etc. |
758124 |
| 3.5.1.97 | more |
Delftia sp. VM4 enzyme structure model of alpha/beta-hydrolase fold protein, overview |
758124 |
| 3.5.1.97 | more |
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 |
-, 757621 |
| 3.5.1.97 | physiological function |
Delftia sp. VM4 can degrade exogenous N-acyl homoserine lactone (AHL), hence it effectively attenuates the virulence of bacterial soft rot pathogen Pectobacterium carotovorum subsp. carotovorum strain BR1 (Pcc BR1) as a consequence of quorum sensing inhibition. Interference of quorum sensing by Delftia sp. VM4 depends on the activity of the N-acylhomoserine lactone-acylase. Delftia sp. VM4 interferes with quorum-sensing signaling of Pcc BR1 when they live commensally in vitro, and such signal interruption causes drastic attenuation of Pcc BR1 virulence determinants. Delftia sp. VM4 cells do not produce an antibiotic-like material to hinder the growth of Pcc BR1 |
758124 |
| 3.5.1.97 | 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 |
-, 757621 |
| 3.5.1.97 | physiological function |
MacQ is a bifunctional enzyme that confers both quorum quenching and antibiotic resistance on strain MRS7. Enzyme N-acylhomoserine lactone acylase (AHL acylase) is responsible for disrupting cell-cell communication (quorum sensing) in bacteria. AHL-mediated virulence factor production in a plant pathogen, Pectobacterium carotovorum, is dramatically attenuated by coculture with MacQ-overexpressing Escherichia coli Origami 2(DE3), whereas Escherichia coli with an empty vector is unable to quench the pathogenicity. MacQ acts as a quorum-quenching enzyme and disrupts the quorum-sensing system in the pathogen. Recombinant MacQ confers multiple beta-lactam antibiotic resistance on an Escherichia coli host strain by hydrolyzing beta-lactam antibiotics |
755847 |
