EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.5.1.97 | more |
virulence of the opportunistic human pathogen is controlled by the N-acyl-homoserine lactone, AHL-dependent quorum-sensing system, the enzyme inactivates AHLs by hydrolysis of the carboxylic side chain with side chain ranging from 11 to 14 C-atoms with broad range specificity, addition of the purified enzyme to cell cultures results in complete inhibition of N-3-oxododecanoyl-(S)-homoserine lactone accumulation and production of the signal molecule 2-heptyl-3-hydroxy-4(1H)-quinolone, as well as reduced production of virulence factors elastase and procyanin |
Pseudomonas aeruginosa |
? |
- |
? |
| 3.5.1.97 | more |
N-acyl-homoserine lactone substrate specificity, no activity with N-butanoyl-(S)-homoserine lactone, N-hexanoyl-(S)-homoserine lactone, and N-3-oxohexanoyl-(S)-homoserine lactone, overview |
Pseudomonas aeruginosa |
? |
- |
? |
| 3.5.1.97 | more |
no activity with penicillin |
Ralstonia sp. |
? |
- |
? |
| 3.5.1.97 | more |
a modified homoserine lactone-o-phthaldialdehyde (HSL-OPA) assay is used to quantify the recombinant AHL acylase activity. No activity is observed with short chain N-acylhomoserine lactones (AHLs), i.e. N-butanoyl-L-homoserine lactone, N-hexanoyl-L-homoserine, or N-(3-oxohexanoyl)-L-homoserine lactone. AHLs of more than ten carbon-acyl chains, i.e. N-decanoyl-L-homoserine lactone and N-dodecanoyl-L-homoserine lactone can not be determined due to their poor solubility |
Ralstonia solanacearum GMI1000 |
? |
- |
? |
| 3.5.1.97 | more |
since the aac gene is predicted as a probable aculeacin A acylase aculeacin A is tested as substrate. The possible products i.e. palmatic acid is not found in the ESI-MS analysis |
Ralstonia solanacearum GMI1000 |
? |
- |
? |
| 3.5.1.97 | more |
N-acyl homoserine lactones, AHLs, with acyl chains ranging from C4 to C14 with or without 3-oxo or 3-hydroxy substituents are all hydrolyzed and inactivated to varying extents, long chain AHLs are generally more susceptible than short chain compounds irrespective of the three position substituent. Ochrobactrum sp. A44 shows a strong preference for inactivating AHLs with the acyl side chains greater than eight carbons and exhibites a slight preference for 3-oxosubstituted AHLs |
Ochrobactrum sp. |
? |
- |
? |
| 3.5.1.97 | more |
no activity towards N-butanoyl-DL-homoserine lactone |
Pseudomonas aeruginosa |
? |
- |
? |
| 3.5.1.97 | more |
PA0305 degrades N-acyl-homoserine lactones with acyl side chains ranging in length from 6 to 14 carbons |
Pseudomonas aeruginosa |
? |
- |
? |
| 3.5.1.97 | more |
the enzyme shows a high level of degrading activity against N-acyl-L-homoserine lactones with long acyl chains but no activity against N-acyl-L-homoserine lactones with acyl chains shorter than eight carbons |
Acinetobacter sp. |
? |
- |
? |
| 3.5.1.97 | more |
enzyme MacQ has the bifunctional capacity to degrade both AHL and beta-lactam antibiotics by deacylation activity (cf. EC 3.5.2.6). MacQ is able to inactivate a variety of beta-lactams, including penicillin derivatives (penicillin G, ampicillin, amoxicillin, and carbenicillin) and cephalosporin derivatives (cephalexin and cefadroxil) |
Acidovorax sp. MR-S7 |
? |
- |
- |
