| Entry |
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| Name |
quorum-quenching N-acyl-homoserine lactonase;
acyl homoserine degrading enzyme;
acyl-homoserine lactone acylase;
AHL lactonase;
AHL-degrading enzyme;
AHL-inactivating enzyme;
AHLase;
AhlD;
AhlK;
AiiA;
AiiA lactonase;
AiiA-like protein;
AiiB;
AiiC;
AttM;
delactonase;
lactonase-like enzyme;
N-acyl homoserine lactonase;
N-acyl homoserine lactone hydrolase;
N-acyl-homoserine lactone lactonase;
N-acyl-L-homoserine lactone hydrolase;
quorum-quenching lactonase;
quorum-quenching N-acyl homoserine lactone hydrolase
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| Class |
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
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| Sysname |
N-acyl-L-homoserine-lactone lactonohydrolase
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| Reaction(IUBMB) |
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine [RN: R08970]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
N-acyl-L-homoserine [CPD: C18061]
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| Comment |
Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes [5]. Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria [5]. N-(3-Oxohexanoyl)-L-homoserine lactone, N-(3-oxododecanoyl)-L-homoserine lactone, N-butanoyl-L-homoserine lactone and N-(3-oxooctanoyl)-L-homoserine lactone can act as substrates [5].
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| History |
EC 3.1.1.81 created 2007
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| Orthology |
| K13075 | N-acyl homoserine lactone hydrolase |
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| Genes |
» show all
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| Reference |
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| Authors |
Thomas PW, Stone EM, Costello AL, Tierney DL, Fast W. |
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| Title |
The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein. |
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| Journal |
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| Reference |
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| Authors |
Dong YH, Gusti AR, Zhang Q, Xu JL, Zhang LH |
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| Title |
Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Wang LH, Weng LX, Dong YH, Zhang LH. |
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| Title |
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase). |
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| Journal |
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| Reference |
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| Authors |
Dong YH, Xu JL, Li XZ, Zhang LH. |
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| Title |
AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora. |
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| Journal |
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| Reference |
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| Authors |
Dong YH, Wang LH, Xu JL, Zhang HB, Zhang XF, Zhang LH. |
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| Title |
Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase. |
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| Journal |
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| Reference |
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| Authors |
Lee SJ, Park SY, Lee JJ, Yum DY, Koo BT, Lee JK. |
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| Title |
Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Park SY, Lee SJ, Oh TK, Oh JW, Koo BT, Yum DY, Lee JK |
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| Title |
AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Ulrich RL. |
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| Title |
Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis. |
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| Journal |
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| Reference |
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| Authors |
Kim MH, Choi WC, Kang HO, Lee JS, Kang BS, Kim KJ, Derewenda ZS, Oh TK, Lee CH, Lee JK. |
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| Title |
The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Liu D, Lepore BW, Petsko GA, Thomas PW, Stone EM, Fast W, Ringe D. |
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| Title |
Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Yang F, Wang LH, Wang J, Dong YH, Hu JY, Zhang LH. |
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| Title |
Quorum quenching enzyme activity is widely conserved in the sera of mammalian species. |
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| Journal |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 3.1.1.81 |
| ExPASy - ENZYME nomenclature database: | 3.1.1.81 |
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