KEGG   ENZYME: 3.5.1.97Help
Entry
EC 3.5.1.97                 Enzyme                                 

Name
acyl-homoserine-lactone acylase;
acyl-homoserine lactone acylase;
AHL-acylase;
AiiD;
N-acyl-homoserine lactone acylase;
PA2385 protein;
quorum-quenching AHL acylase;
quorum-quenching enzyme;
PvdQ;
QuiP
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
N-acyl-L-homoserine-lactone amidohydrolase
Reaction(IUBMB)
an N-acyl-L-homoserine lactone + H2O = L-homoserine lactone + a carboxylate [RN:R09646]
Reaction(KEGG)
Substrate
N-acyl-L-homoserine lactone [CPD:C18049];
H2O [CPD:C00001]
Product
L-homoserine lactone [CPD:C19777];
carboxylate [CPD:C00060]
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. 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. This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine lactone ring of AHL-dependent quorum-sensing signal molecules [1]. It has broad specificity for AHLs with side changes ranging in length from 11 to 14 carbons. Substituents at the 3'-position, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity [1].
History
EC 3.5.1.97 created 2007
Orthology
K07116  
acyl-homoserine-lactone acylase
Genes
PLU: 
XNE: 
PSI: 
DJI: 
VFU: 
PAE: 
PA1032(quiP) PA2385(pvdQ)
PAEV: 
N297_1068(quiP) N297_2458(pvdQ)
PAU: 
PAP: 
PAG: 
PAF: 
PNC: 
PDK: 
PSG: 
PRP: 
PAEP: 
PAER: 
PAEM: 
PAEL: 
PAES: 
PAEU: 
BN889_01091(quiP_2) BN889_01092(quiP_3) BN889_02613(pvdQ)
PAEG: 
PAEC: 
M802_1065(quiP) M802_2455(pvdQ)
PPU: 
PPF: 
PPG: 
PPW: 
PPT: 
PPB: 
PPI: 
PPX: 
PPUH: 
PPUT: 
PPUN: 
PP4_10510(quiP) PP4_29180(pvdQ)
PPUU: 
PST: 
PSB: 
PSYR: 
PSP: 
PCI: 
PFL: 
PFL_1268(quiP) PFL_2902(pvdQ)
PPRC: 
PFO: 
PFS: 
PFE: 
PFC: 
PPZ: 
PEN: 
PMY: 
PMK: 
PSA: 
PSZ: 
PSR: 
PSC: 
PSJ: 
PSH: 
PBA: 
PFV: 
PDR: 
PRE: 
PSV: 
PSK: 
PMON: 
PMOT: 
PKC: 
PKB_1465(quiP)
CJA: 
AVN: 
AVL: 
AVD: 
PCR: 
PSO: 
SON: 
SO_0918(aaiD)
SFR: 
SAZ: 
SBL: 
SBM: 
SBT: 
SBS: 
SBB: 
SPC: 
SHP: 
SHE: 
SHM: 
SHN: 
SHW: 
SWD: 
SWP: 
SVO: 
PSM: 
MAD: 
HP15_1139(pvdQ)
AMC: 
AMAC: 
AMB: 
AMG: 
AMH: 
AMK: 
AMAA: 
AMAL: 
AMAE: 
AMAO: 
AMAD: 
AMAI: 
AMAG: 
ALT: 
GNI: 
GPS: 
FBL: 
HCH: 
ADI: 
AHY: 
GPB: 
RSO: 
RSc2547(aac)
RSM: 
RSE: 
RPI: 
RPF: 
RME: 
BGL: 
BGD: 
BYI: 
BUO: 
AXY: 
AAV: 
DIA: 
AAA: 
ACK: 
DAC: 
DEL: 
VAP: 
VPE: 
VPD: 
DOL: 
MXA: 
MSD: 
CCX: 
SUR: 
SCU: 
HOH: 
PLA: 
BME: 
CCR: 
HNE: 
SAL: 
ELI: 
TMO: 
TMO_b0330(pvdQ)
BSUB: 
SGR: 
SCB: 
SFA: 
SBH: 
SVE: 
SDV: 
STRP: 
SFI: 
NCA: 
SRO: 
AMD: 
AMN: 
AMM: 
AMZ: 
AOI: 
AMI: 
KAL: 
STP: 
SAQ: 
AMS: 
AYM: 
TPX: 
TRS: 
GBA: 
SYN: 
SYZ: 
SYY: 
SYNGTS_2134(slr0378)
SYT: 
SYNGTI_2133(slr0378)
SYS: 
SYNPCCN_2132(slr0378)
SYQ: 
SYNPCCP_2132(slr0378)
CYT: 
CYP: 
CYC: 
CYH: 
CYJ: 
GLP: 
OAC: 
ONI: 
CEP: 
MIC: 
NPU: 
NOS: 
AVA: 
CSG: 
CALT: 
CTHE: 
PLP: 
SCS: 
SRU: 
SRM: 
SGN: 
CMR: 
RSI: 
EOL: 
MTT: 
RBI: 
DRA: 
DGO: 
DPD: 
 » show all
Taxonomy
Reference
1  [PMID:16495538]
  Authors
Sio CF, Otten LG, Cool RH, Diggle SP, Braun PG, Bos R, Daykin M, Camara M, Williams P, Quax WJ.
  Title
Quorum quenching by an N-acyl-homoserine lactone acylase from Pseudomonas aeruginosa PAO1.
  Journal
Infect. Immun. 74 (2006) 1673-82.
  Organism
Pseudomonas aeruginosa
  Sequence
[pae:PA2385]
Reference
2  [PMID:12535081]
  Authors
Lin YH, Xu JL, Hu J, Wang LH, Ong SL, Leadbetter JR, Zhang LH.
  Title
Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes.
  Journal
Mol. Microbiol. 47 (2003) 849-60.
  Organism
Ralstonia sp.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

DBGET integrated database retrieval system