KEGG   ENZYME: 3.1.1.81Help
Entry
EC 3.1.1.81                 Enzyme                                 

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
Class
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
BRITE hierarchy
Sysname
N-acyl-L-homoserine-lactone lactonohydrolase
Reaction(IUBMB)
an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine [RN:R08970]
Reaction(KEGG)
Substrate
N-acyl-L-homoserine lactone [CPD:C18049];
H2O [CPD:C00001]
Product
N-acyl-L-homoserine [CPD:C18061]
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].
History
EC 3.1.1.81 created 2007
Orthology
K13075  
N-acyl homoserine lactone hydrolase
Genes
PSC: 
PSH: 
AFI: 
THI: 
RLI: 
BAE: 
BAN: 
BAR: 
BAT: 
BAH: 
BAI: 
BAX: 
BANT: 
BANR: 
BAL: 
BCE: 
BCA: 
BCZ: 
BCR: 
BCB: 
BCU: 
BCG: 
BCQ: 
BCX: 
BNC: 
BCF: 
BCER: 
BTK: 
BTL: 
BTB: 
BTT: 
BTC: 
BTF: 
BTM: 
BTG: 
BTI: 
BTN: 
BTHT: 
BTHU: 
BWE: 
BTY: 
PPY: 
PPM: 
PPO: 
PPM_2544(hagH) PPM_3486(M1_3854)
PPOL: 
CKL: 
CKR: 
ACH: 
KFL: 
MMAR: 
ACTN: 
HAU: 
 » show all
Taxonomy
Reference
1  [PMID:15895999]
  Authors
Thomas PW, Stone EM, Costello AL, Tierney DL, Fast W.
  Title
The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein.
  Journal
Biochemistry. 44 (2005) 7559-69.
  Organism
Bacillus thuringiensis
  Sequence
Reference
2  [PMID:11916693]
  Authors
Dong YH, Gusti AR, Zhang Q, Xu JL, Zhang LH.
  Title
Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species.
  Journal
Appl. Environ. Microbiol. 68 (2002) 1754-9.
  Organism
Bacillus species
  Sequence
Reference
3  [PMID:14734559]
  Authors
Wang LH, Weng LX, Dong YH, Zhang LH.
  Title
Specificity and enzyme kinetics of the quorum-quenching N-Acyl homoserine lactone lactonase (AHL-lactonase).
  Journal
J. Biol. Chem. 279 (2004) 13645-51.
  Organism
Bacillus sp.
  Sequence
Reference
4  [PMID:10716724]
  Authors
Dong YH, Xu JL, Li XZ, Zhang LH.
  Title
AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 3526-31.
  Organism
Bacillus sp. 240B1
  Sequence
Reference
5  [PMID:11459062]
  Authors
Dong YH, Wang LH, Xu JL, Zhang HB, Zhang XF, Zhang LH.
  Title
Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase.
  Journal
Nature. 411 (2001) 813-7.
  Organism
Bacillus sp.
  Sequence
Reference
6  [PMID:12147491]
  Authors
Lee SJ, Park SY, Lee JJ, Yum DY, Koo BT, Lee JK.
  Title
Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis.
  Journal
Appl. Environ. Microbiol. 68 (2002) 3919-24.
  Organism
Bacillus thuringiensis
  Sequence
Reference
7  [PMID:12777494]
  Authors
Park SY, Lee SJ, Oh TK, Oh JW, Koo BT, Yum DY, Lee JK.
  Title
AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria.
  Journal
Microbiology. 149 (2003) 1541-50.
  Organism
Arthrobacter sp.
  Sequence
[up:Q7X3T2]
Reference
8  [PMID:15466564]
  Authors
Ulrich RL.
  Title
Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis.
  Journal
Appl. Environ. Microbiol. 70 (2004) 6173-80.
Reference
9  [PMID:16314577]
  Authors
Kim MH, Choi WC, Kang HO, Lee JS, Kang BS, Kim KJ, Derewenda ZS, Oh TK, Lee CH, Lee JK.
  Title
The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17606-11.
  Organism
Bacillus thuringiensis
  Sequence
Reference
10 [PMID:16087890]
  Authors
Liu D, Lepore BW, Petsko GA, Thomas PW, Stone EM, Fast W, Ringe D.
  Title
Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 11882-7.
  Organism
Bacillus thuringiensis
  Sequence
Reference
11 [PMID:15963993]
  Authors
Yang F, Wang LH, Wang J, Dong YH, Hu JY, Zhang LH.
  Title
Quorum quenching enzyme activity is widely conserved in the sera of mammalian species.
  Journal
FEBS. Lett. 579 (2005) 3713-7.
  Organism
Mus musculus, Homo sapiens
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
389867-43-0

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