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].
Orthology
K13075  
N-acyl homoserine lactone hydrolase
Genes
PSC: 
PSH: 
AFI: 
THI: 
RLI: 
BAE: 
BAN: 
BAR: 
BAT: 
BAH: 
BAI: 
BAA_3546
BAX: 
H9401_3344
BAL: 
BACI_c34120
BCE: 
BC3453
BCA: 
BCE_3466
BCZ: 
BCZK3174
BCR: 
BCAH187_A3485
BCB: 
BCB4264_A3458
BCU: 
BCAH820_3474
BCG: 
BCG9842_B1790
BCQ: 
BCQ_3259
BCX: 
BCA_3538
BNC: 
BCN_3276
BCF: 
bcf_17080
BCER: 
BCK_17970
BTK: 
BT9727_3232
BTL: 
BALH_3106
BTB: 
BMB171_C3134
BTT: 
HD73_3697
BTC: 
CT43_CH3389
BTF: 
YBT020_16950
BTM: 
MC28_2602
BTG: 
BTB_c35230(aiiA)
BTI: 
BTG_02315
BTN: 
BTF1_14555
BTHT: 
H175_ch3442
BWE: 
BcerKBAB4_3166
PPY: 
PPE_02477
PPM: 
PPSC2_c3697
PPO: 
PPM_2544(hagH)
CKL: 
CKL_2599
CKR: 
CKR_2305
ACH: 
Achl_3366
KFL: 
Kfla_1531
MMAR: 
MODMU_2622(attM)
HAU: 
Haur_0903
 » 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 [GN:btk btl]
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
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.
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
NCBI-GI: 7416988
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.
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.
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.
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.
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.
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.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
389867-43-0
DBGET integrated database retrieval system