KEGG   ENZYME: 3.1.1.2Help
Entry
EC 3.1.1.2                  Enzyme                                 

Name
arylesterase;
A-esterase;
paraoxonase;
aromatic esterase
Class
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
BRITE hierarchy
Sysname
aryl-ester hydrolase
Reaction(IUBMB)
a phenyl acetate + H2O = a phenol + acetate [RN:R07342]
Reaction(KEGG)
Substrate
phenyl acetate [CPD:C15583];
H2O [CPD:C00001]
Product
phenol [CPD:C15584];
acetate [CPD:C00033]
Comment
Acts on many phenolic esters. The reactions of EC 3.1.8.1 aryldialkylphosphatase, were previously attributed to this enzyme. It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases [7,8]. The natural substrates of the paraoxonases are lactones [7,8], with (+/-)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate [8].
History
EC 3.1.1.2 created 1961, modified 1989
Pathway
ec00363  Bisphenol degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K01045  arylesterase / paraoxonase
Genes
HSA: 5444(PON1) 5445(PON2) 5446(PON3)
PTR: 463547(PON1) 463548(PON3) 463549(PON2)
PPS: 100971627(PON1) 100971959(PON3) 100972315(PON2)
GGO: 101146649(PON1) 101147009(PON3) 101147360(PON2) 109027758
PON: 100436262(PON3) 100436640(PON1) 100437018(PON2)
NLE: 100602768(PON1) 100603110(PON3) 100603799(PON2)
MCC: 699107(PON2) 699236(PON3) 699355(PON1)
MCF: 102119827(PON2) 102120476(PON3) 102121098(PON1)
CSAB: 103226525(PON3) 103226526(PON2) 103226528(PON1)
RRO: 104656585(PON1) 104656587(PON3) 104656588(PON2)
RBB: 108513529(PON2) 108513530(PON3) 108513531(PON1)
CJC: 100407939(PON2) 100408549(PON3) 100408915(PON1)
SBQ: 101047829(PON3) 101048148(PON2) 101048681(PON1)
MMU: 18979(Pon1) 269823(Pon3) 330260(Pon2)
RNO: 296851(Pon2) 312086(Pon3) 84024(Pon1)
CGE: 100762244(Pon1) 100762539(Pon2) 100762826(Pon3)
NGI: 103725227(Pon3) 103725228(Pon2) 103725260(Pon1)
HGL: 101696947(Pon1) 101697319(Pon3) 101697694(Pon2)
OCU: 100008754(PON3) 100009133(PON1) 100340152(PON2)
TUP: 102467949(PON3) 102482718(PON2) 102503295(PON1)
CFA: 403855(PON2) 475234(PON1) 475235(PON3)
AML: 100466658(PON2) 100467410(PON1) 100467660(PON3)
UMR: 103658742(PON1) 103658743(PON3) 103658801(PON2)
ORO: 101371249(PON2) 101371749(PON3) 101372042(PON1)
FCA: 101091522(PON1) 101091774(PON3) 101094492(PON2)
PTG: 102965359(PON2) 102969631(PON3) 102969909(PON1)
BTA: 281417(PON2) 510953(PON3) 523798(PON1)
BOM: 102268223(PON1) 102268513(PON3) 102269334(PON2)
BIU: 109558220(PON1) 109558221(PON3) 109558222(PON2)
PHD: 102326568(PON1) 102326932(PON3) 102331586(PON2)
CHX: 102183658(PON2) 102189091(PON1) 102189455(PON3)
OAS: 100145861(PON2) 100337686(PON3) 101116983(PON1)
SSC: 100048952(PON1) 100142663(PON2) 733674(PON3)
CFR: 102519221(PON3) 102519463(PON1) 102521631(PON2)
CDK: 105088724(PON2) 105088725(PON3) 105088728(PON1)
BACU: 103002002(PON2) 103002453(PON3) 103004502(PON1)
LVE: 103072098(PON3) 103072365(PON2) 103075141(PON1) 103079171
OOR: 101286851(PON2) 101287293(PON3)
ECB: 100051896(PON1) 100051959(PON3) 100062686(PON2)
EPZ: 103541442(PON1) 103542649(PON3) 103542650(PON2) 103566405
EAI: 106838926(PON2) 106838927(PON3) 106838928(PON1)
MYB: 102249558(PON3) 102250151(PON1) 102251833(PON2)
MYD: 102757128(PON2) 102772860(PON1) 102775231(PON3)
HAI: 109393132 109393133(PON1)
LAV: 100667197(PON2) 100675274(PON3) 100675554(PON1)
MDO: 100017970(PON2) 100018559(PON3) 100028798
OAA: 103168141
GGA: 395830(PON2)
MGP: 100303695(PON2)
CJO: 107309112(PON2)
APLA: 101800414(PON2)
ACYG: 106037501(PON2)
TGU: 100218152(PON2)
GFR: 102033037(PON2)
FAB: 101812552(PON2)
PHI: 102101075(PON2)
PMAJ: 107200070
CCAE: 111924234
CCW: 104689162
FPG: 101913744(PON2)
FCH: 102055053(PON2)
CLV: 102089494
EGZ: 104128625
AAM: 106483521(PON2)
ASN: 102370400
AMJ: 102569523(PON2)
PSS: 102457846
CMY: 102930790(PON2)
CPIC: 101938475(PON2)
ACS: 100551677(pon2)
PVT: 110074724
PBI: 103052672
GJA: 107118000(PON2)
XLA: 108718843 380341(pon2.L) 432039(pon2.S)
XTR: 448598(pon2)
DRE: 335176(pon2) 554122(pon3.1) 568655(pon3.2)
IPU: 108271509
AMEX: 103046166
TRU: 101062836
CSEM: 103388494
SFM: 108940718
LCM: 102361851
CMK: 103176917
OBI: 106873488
HMG: 100211341
AQU: 105316431
SSCK: SPSK_02462
PSPI: PS2015_622
 » show all
Taxonomy
Reference
1  [PMID:13032041]
  Authors
ALDRIDGE WN.
  Title
Serum esterases.  I.  Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination.
  Journal
Biochem J 53:110-7 (1953)
Reference
2  [PMID:13638253]
  Authors
AUGUSTINSSON KB, OLSSON B.
  Title
Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies.
  Journal
Biochem J 71:477-84 (1959)
Reference
3  [PMID:5047702]
  Authors
Bosmann HB.
  Title
Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate.
  Journal
Biochim Biophys Acta 276:180-91 (1972)
DOI:10.1016/0005-2744(72)90019-8
Reference
4  [PMID:2152179]
  Authors
Kim DH, Yang YS, Jakoby WB.
  Title
Nonserine esterases from rat liver cytosol.
  Journal
Protein Expr Purif 1:19-27 (1990)
DOI:10.1016/1046-5928(90)90040-6
Reference
5  [PMID:2822017]
  Authors
Mackness MI, Thompson HM, Hardy AR, Walker CH.
  Title
Distinction between 'A'-esterases and arylesterases. Implications for esterase classification.
  Journal
Biochem J 245:293-6 (1987)
Reference
6
  Authors
In: Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Eds.), Enzymes Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester, UK, 1989.
Reference
7  [PMID:15835926]
  Authors
Khersonsky O, Tawfik DS.
  Title
Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase.
  Journal
Biochemistry 44:6371-82 (2005)
DOI:10.1021/bi047440d
Reference
8  [PMID:15772423]
  Authors
Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN.
  Title
Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities.
  Journal
J Lipid Res 46:1239-47 (2005)
DOI:10.1194/jlr.M400511-JLR200
  Sequence
[hsa:5444 5445 5446]
Other DBs
ExplorEnz - The Enzyme Database: 3.1.1.2
IUBMB Enzyme Nomenclature: 3.1.1.2
ExPASy - ENZYME nomenclature database: 3.1.1.2
UM-BBD (Biocatalysis/Biodegradation Database): 3.1.1.2
BRENDA, the Enzyme Database: 3.1.1.2
CAS: 9032-73-9

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
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
KPE: KPK_2642(ahlK)
KPJ: N559_2565
KPX: PMK1_04076(attM)
KPNU: LI86_12785
KPNK: BN49_2831
KVA: Kvar_2597
YIN: CH53_198(attM)
SRL: SOD_c29960(attM)
PLU: plu2238
PAY: PAU_00481(attM_aiiB)
PPUT: L483_14615
PKC: PKB_2170
TCX: Tcr_1803
SALN: SALB1_0442
THI: THI_3692
ATU: Atu5139(blcC) Atu6071(aiiB)
ATF: Ach5_48250(blcC)
AVI: Avi_1654(attM)
RLE: pRL100136
RHT: NT26_2252
VGO: GJW-30_1_04057(attM)
AZC: AZC_0767
MMED: Mame_00111
RBM: TEF_00480
SMAZ: LH19_12320
BLAS: BSY18_3630
ACR: Acry_1421
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
SHA: SH0372
SSP: SSP0236
SCA: SCA_2373
SPAS: STP1_1768
PPY: PPE_02477
PPO: PPM_2544(hagH) PPM_3486(M1_3854)
PPOL: X809_29690
PRI: PRIO_3470(aiiB)
SIV: SSIL_0083
JEO: JMA_35210
CBE: Cbei_2104
CBZ: Cbs_2104
CBEI: LF65_02416
CKL: CKL_2599
CKR: CKR_2305
SLP: Slip_0667
TMR: Tmar_1805
MMC: Mmcs_1848
MKM: Mkms_1895
MJL: Mjls_1829
MPHL: MPHLCCUG_01980(aiiA_2)
RHS: A3Q41_02946(aiiA_1)
SBH: SBI_01436
SFI: SFUL_4208
SALU: DC74_1424
SALL: SAZ_07650
STRE: GZL_07793
SMAL: SMALA_2158
SLAU: SLA_1021
ACH: Achl_3366
ACIJ: JS278_01978(aiiA)
KFL: Kfla_1531
PSIM: KR76_17560
MMAR: MODMU_1792 MODMU_2622(attM)
PSEA: WY02_11680
PSEH: XF36_01905
ACTN: L083_6939
AFS: AFR_36705
PDO: PSDT_0696
TBI: Tbis_2162
RXY: Rxyl_2378
HAU: Haur_0903
STI: Sthe_0932
CHZ: CHSO_1918
MEB: Abm4_1039
MFC: BRM9_0533
TVO: TVG1350001(TVG1350001)
FAI: FAD_0985
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
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
ASC: ASAC_0699
ACIA: SE86_00615
 » 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 44:7559-69 (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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