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
Bisphenol degradation
Metabolic pathways
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: 
PON: 
100436262(PON3) 100436640(PON1) 100437018(PON2)
MCC: 
699107(PON2) 699236(PON3) 699355(PON1)
MCF: 
102119827(PON2) 102120476(PON3) 102121098(PON1)
MMU: 
18979(Pon1) 269823(Pon3) 330260(Pon2)
RNO: 
296851(Pon2) 312086(Pon3) 84024(Pon1)
CGE: 
100762244(Pon1) 100762539(Pon2) 100762826(Pon3)
HGL: 
101696947(Pon1) 101697319(Pon3) 101697694(Pon2)
TUP: 
102467949(PON3) 102482718(PON2) 102503295(PON1)
CFA: 
403855(PON2) 475234(PON1) 475235(PON3)
AML: 
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)
PHD: 
102326568(PON1) 102326932(PON3) 102331586(PON2)
CHX: 
102183658(PON2) 102189091(PON1) 102189455(PON3)
OAS: 
100145861(PON2) 100337686(PON3) 101116983(PON1)
SSC: 
CFR: 
102519221(PON3) 102519463(PON1) 102521631(PON2)
BACU: 
103002002(PON2) 103002453(PON3) 103004502(PON1)
LVE: 
ECB: 
100051896(PON1) 100051959(PON3) 100062686(PON2)
MYB: 
102249558(PON3) 102250151(PON1) 102251833(PON2)
MYD: 
102757128(PON2) 102772860(PON1) 102775231(PON3)
PALE: 
102878821(PON1) 102879084(PON3) 102879651(PON2)
MDO: 
SHR: 
100922843(PON2) 100929514(PON3)
OAA: 
GGA: 
395830(PON2)
MGP: 
100303695(PON2)
APLA: 
101800414(PON2)
TGU: 
100218152(PON2)
FAB: 
101812552(PON2)
PHI: 
102101075(PON2)
FPG: 
101913744(PON2)
FCH: 
102055053(PON2)
CLV: 
102089494(PON2)
ASN: 
102370400(PON2)
AMJ: 
102569523(PON2)
PSS: 
102457846(PON2)
CMY: 
102930790(PON2)
ACS: 
100551677(pon2)
PBI: 
103052672(PON2)
XLA: 
XTR: 
448598(pon2)
DRE: 
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
SPU: 
LOA: 
NVE: 
HMG: 
YLI: 
GTR: 
PGR: 
EHX: 
MSD: 
 » 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 (1953) 110-7.
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 (1959) 477-84.
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 (1972) 180-91.
Reference
4  [PMID:2152179]
  Authors
Kim DH, Yang YS, Jakoby WB.
  Title
Nonserine esterases from rat liver cytosol.
  Journal
Protein. Expr. Purif. 1 (1990) 19-27.
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 (1987) 293-6.
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 (2005) 6371-82.
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 (2005) 1239-47.
  Sequence
[hsa:5444 5445 5446]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
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
PSC: 
PSH: 
AFI: 
THI: 
RLI: 
BAE: 
BAN: 
BAR: 
BAT: 
BAH: 
BAI: 
BAX: 
BANT: 
BANR: 
BANS: 
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: 
BMYC: 
DJ92_391(aiiA)
PPY: 
PPM: 
PPO: 
PPM_2544(hagH) PPM_3486(M1_3854)
PPOL: 
PPQ: 
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.
  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.
  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.
  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.
  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.
  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.
  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.
  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.
  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.
  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.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
389867-43-0

KEGG   ENZYME: 3.1.8.1Help
Entry
EC 3.1.8.1                  Enzyme                                 

Name
aryldialkylphosphatase;
organophosphate hydrolase;
paraoxonase;
A-esterase;
aryltriphosphatase;
organophosphate esterase;
esterase B1;
esterase E4;
paraoxon esterase;
pirimiphos-methyloxon esterase;
OPA anhydrase;
organophosphorus hydrolase;
phosphotriesterase;
paraoxon hydrolase;
OPH;
organophosphorus acid anhydrase
Class
Hydrolases;
Acting on ester bonds;
Phosphoric-triester hydrolases
BRITE hierarchy
Sysname
aryltriphosphate dialkylphosphohydrolase
Reaction(IUBMB)
an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol [RN:R03979]
Reaction(KEGG)
R03979 > R05548;
(other) R05421
Show
Substrate
aryl dialkyl phosphate [CPD:C03254];
H2O [CPD:C00001]
Product
dialkyl phosphate [CPD:C02534];
phenol [CPD:C15584]
Comment
Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. Inhibited by chelating agents; requires divalent cations for activity. Previously regarded as identical with EC 3.1.1.2 arylesterase.
History
EC 3.1.8.1 created 1989
Pathway
Aminobenzoate degradation
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: 
PON: 
100436262(PON3) 100436640(PON1) 100437018(PON2)
MCC: 
699107(PON2) 699236(PON3) 699355(PON1)
MCF: 
102119827(PON2) 102120476(PON3) 102121098(PON1)
MMU: 
18979(Pon1) 269823(Pon3) 330260(Pon2)
RNO: 
296851(Pon2) 312086(Pon3) 84024(Pon1)
CGE: 
100762244(Pon1) 100762539(Pon2) 100762826(Pon3)
HGL: 
101696947(Pon1) 101697319(Pon3) 101697694(Pon2)
TUP: 
102467949(PON3) 102482718(PON2) 102503295(PON1)
CFA: 
403855(PON2) 475234(PON1) 475235(PON3)
AML: 
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)
PHD: 
102326568(PON1) 102326932(PON3) 102331586(PON2)
CHX: 
102183658(PON2) 102189091(PON1) 102189455(PON3)
OAS: 
100145861(PON2) 100337686(PON3) 101116983(PON1)
SSC: 
CFR: 
102519221(PON3) 102519463(PON1) 102521631(PON2)
BACU: 
103002002(PON2) 103002453(PON3) 103004502(PON1)
LVE: 
ECB: 
100051896(PON1) 100051959(PON3) 100062686(PON2)
MYB: 
102249558(PON3) 102250151(PON1) 102251833(PON2)
MYD: 
102757128(PON2) 102772860(PON1) 102775231(PON3)
PALE: 
102878821(PON1) 102879084(PON3) 102879651(PON2)
MDO: 
SHR: 
100922843(PON2) 100929514(PON3)
OAA: 
GGA: 
395830(PON2)
MGP: 
100303695(PON2)
APLA: 
101800414(PON2)
TGU: 
100218152(PON2)
FAB: 
101812552(PON2)
PHI: 
102101075(PON2)
FPG: 
101913744(PON2)
FCH: 
102055053(PON2)
CLV: 
102089494(PON2)
ASN: 
102370400(PON2)
AMJ: 
102569523(PON2)
PSS: 
102457846(PON2)
CMY: 
102930790(PON2)
ACS: 
100551677(pon2)
PBI: 
103052672(PON2)
XLA: 
XTR: 
448598(pon2)
DRE: 
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
SPU: 
LOA: 
NVE: 
HMG: 
YLI: 
GTR: 
PGR: 
EHX: 
MSD: 
 » 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 (1953) 110-7.
Reference
2  [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 (1972) 180-91.
Reference
3  [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 (1987) 293-6.
Reference
4  [PMID:14420012]
  Authors
MAIN AR.
  Title
The differentiation of the A-type esterases in sheep serum.
  Journal
Biochem. J. 75 (1960) 188-95.
Reference
5
  Authors
In: Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Eds.), Enzymes Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester, UK, 1989.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
117698-12-1

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