KEGG   ENZYME: 3.1.1.81
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
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)
R08970
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
EEC: EcWSU1_02559(attM)
ELG: BH714_08635
KPN: KPN_01736
KPU: KP1_2781
KPM: KPHS_26830
KPP: A79E_2497
KPH: KPNIH24_14910
KPV: KPNIH29_13485
KPW: KPNIH30_13810
KPG: KPNIH32_13655
KPJ: N559_2565
KPX: PMK1_04076(attM)
KPNU: LI86_12785
KPNK: BN49_2831
KVA: Kvar_2597
KPE: KPK_2642(ahlK)
CLAP: NCTC11466_02926(attM)
METY: MRY16398_32520(attM)
YIN: CH53_198(attM)
SRL: SOD_c29960(attM)
PLU: plu2238
PAY: PAU_00481(attM_aiiB)
MHQ: D650_3190
MHAT: B824_5600
MHAM: J450_05805
MHAL: N220_12605
MHAQ: WC39_01645
MHAY: VK67_01650
MVR: X781_5130
BTRA: F544_400
LEM: LEN_4408
PPUT: L483_14615
PPUD: DW66_3552
PKC: PKB_2170
SAZ: Sama_0157
SKH: STH12_03839(gloB_4)
TCX: Tcr_1803
HMAR: HVMH_0664
SALN: SALB1_0442
BCJ: BCAS0689
BCEW: DM40_5391
BDL: AK34_5589
BLAT: WK25_17630
BMEC: WJ16_19650
CABA: SBC2_54240(Y2-aiiA)
AXX: ERS451415_03553(aiiA)
PVAC: HC248_02610(aiiA)
JAG: GJA_4994
THI: THI_3692
MPAU: ZMTM_08640
SLAC: SKTS_01910
DVL: Dvul_0948
DVM: DvMF_3180
DDE: Dde_1331
DFL: DFE_0335
DPI: BN4_12612
DPS: DP0452
DSF: UWK_03209
MXA: MXAN_7313
SFU: Sfum_3579
DBR: Deba_2199
MES: Meso_2405
RBS: RHODOSMS8_01313(attM)
ATU: Atu5139(blcC) Atu6071(aiiB)
ATF: Ach5_48250(blcC)
AVI: Avi_1654(attM)
RLE: pRL100136
NEN: NCHU2750_42650(ahlD) NCHU2750_56090(ahlD)
SHZ: shn_28555
BRS: S23_31620(attM)
AOL: S58_69970
BRAD: BF49_6528
VGO: GJW-30_1_04057(attM)
AZC: AZC_0767
RBM: TEF_00480
TSV: DSM104635_03525(attM)
RUT: FIU92_00175(Y2-aiiA2)
RDE: RD1_0080
HNE: HNE_3377
SAL: Sala_2130
SMAZ: LH19_12320
SWI: Swit_4708
SPHD: HY78_01595
SPHM: G432_17335
SSAN: NX02_05840
SPKC: KC8_18325
SSY: SLG_16390
ACR: Acry_1421
SHUM: STHU_22390
BAN: BA_3514
BAR: GBAA_3514
BAT: BAS3259
BAI: BAA_3546
BANT: A16_35260
BANR: A16R_35690
BANS: BAPAT_3364
BANV: DJ46_2242(aiiA)
BCE: BC3453
BCA: BCE_3466
BCQ: BCQ_3259
BCX: BCA_3538
BNC: BCN_3276
BCF: bcf_17080
BCER: BCK_17970
BTL: BALH_3106
BTT: HD73_3697
BTHI: BTK_18210
BTM: MC28_2602(aiiA)
BTG: BTB_c35230(aiiA)
BTI: BTG_02315
BTW: BF38_4619(aiiA)
BWW: bwei_1484(aiiA)
BMYO: BG05_2551(aiiA) BG05_5611(aiiA)
BMYC: DJ92_391(aiiA)
BMEG: BG04_5254(aiiB)
ANM: GFC28_253(aiiB)
ANL: GFC29_1371(aiiB)
LSP: Bsph_3377
PASA: BAOM_2524
SHA: SH0372
SSP: SSP0236
SCA: SCA_2373
SPIC: SAMEA4384060_0114(aiiB)
SSIM: SAMEA4384339_1823(attM)
PPY: PPE_02477
PPO: PPM_2544(hagH) PPM_3486(M1_3854)
PPOL: X809_29690
PRI: PRIO_3470(aiiB)
BTS: Btus_1282
SIV: SSIL_0083
JEO: JMA_35210
CKL: CKL_2599
CKR: CKR_2305
ROB: CK5_34240
SLP: Slip_0667
PTH: PTH_2407
TMR: Tmar_1805
MMC: Mmcs_1848
MKM: Mkms_1895
MJL: Mjls_1829
MPHL: MPHLCCUG_01980(aiiA_2)
MAUU: NCTC10437_01927(aiiA_1) NCTC10437_02782(aiiA_2)
MMAG: MMAD_20310
MAIC: MAIC_29990(attM)
MTY: MTOK_49270(attM)
MARZ: MARA_20090(attM)
MHEV: MHEL_53810(attM)
MSAR: MSAR_38630
MANY: MANY_15700
MAUB: MAUB_11530(attM)
MPHU: MPHO_01610(attM)
MMAT: MMAGJ_30450(attM)
MBOK: MBOE_52260
NFA: NFA_55920
NFR: ERS450000_04269(attM)
RHS: A3Q41_02946(aiiA_1)
SMAL: SMALA_2158
SBH: SBI_01436
SFI: SFUL_4208
SALU: DC74_1424
SALL: SAZ_07650
STRE: GZL_07793
SLD: T261_7407
SLAU: SLA_1021
SGE: DWG14_00131(aiiA)
SNF: JYK04_08032(attM)
MLV: CVS47_02657(aiiA)
ACH: Achl_3366
ACIJ: JS278_01978(aiiA)
NCA: Noca_0090
PSIM: KR76_17560
KFL: Kfla_1531
TBI: Tbis_2162
MMAR: MODMU_1792 MODMU_2622(attM)
PSEA: WY02_11680
PSEH: XF36_01905
PAUT: Pdca_25920
ALO: CRK61459
PDO: PSDT_0696
HAU: Haur_0903
OTE: Oter_1858
LIC: LIC_10092
LBJ: LBJ_0107
LBF: LBF_1053
SDJ: NCTC13534_03077(attM)
FAE: FAES_2391
DDO: I597_0981(attM)
MLT: VC82_1454
MESQ: C7H62_0905
CHZ: CHSO_1918
TLE: Tlet_0154
MARN: LN42_07885
KOL: Kole_1923
MAE: Maeo_0442
MMIL: sm9_1073
MEYE: TL18_06495
METH: MBMB1_1311
MCUB: MCBB_1541
GAC: GACE_1504
HAL: VNG_1340C
HSL: OE_2913R
HHB: Hhub_4037
HMA: rrnAC1263
HHI: HAH_1858
NPH: NP_3970A
HVO: HVO_1368
HLA: Hlac_2721
HTU: Htur_1316
SALI: L593_07165
TVO: TVG1350001(TVG1350001)
PTO: PTO1044
FAI: FAD_0985
MARC: AR505_0071
SSO: SSO1537
SOL: Ssol_2373
SSOA: SULA_2400
SSOL: SULB_2401
SSOF: SULC_2398
SID: M164_0496
SII: LD85_0968
SIH: SiH_0769
SIR: SiRe_0574
SIC: SiL_0593
VDI: Vdis_0557
ASC: ASAC_0699
ACIA: SE86_00615
 » show all
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 44:7559-69 (2005)
DOI:10.1021/bi050050m
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 68:1754-9 (2002)
DOI:10.1128/AEM.68.4.1754-1759.2002
  Sequence
[btt:HD73_3697]
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 279:13645-51 (2004)
DOI:10.1074/jbc.M311194200
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 97:3526-31 (2000)
DOI:10.1073/pnas.060023897
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 411:813-7 (2001)
DOI:10.1038/35081101
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 68:3919-24 (2002)
DOI:10.1128/AEM.68.8.3919-3924.2002
  Sequence
[btt:HD73_3697]
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 149:1541-50 (2003)
DOI:10.1099/mic.0.26269-0
  Sequence
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 70:6173-80 (2004)
DOI:10.1128/AEM.70.10.6173-6180.2004
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 102:17606-11 (2005)
DOI:10.1073/pnas.0504996102
  Sequence
[btt:HD73_3697]
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 102:11882-7 (2005)
DOI:10.1073/pnas.0505255102
  Sequence
[btt:HD73_3697]
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 579:3713-7 (2005)
DOI:10.1016/j.febslet.2005.05.060
Other DBs
ExplorEnz - The Enzyme Database: 3.1.1.81
IUBMB Enzyme Nomenclature: 3.1.1.81
ExPASy - ENZYME nomenclature database: 3.1.1.81
BRENDA, the Enzyme Database: 3.1.1.81
CAS: 389867-43-0

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