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)
CCAN: 109693468 109693469
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)
AJU: 106969955 106969956 106970003
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)
RSS: 109446396 109446397
PALE: 102878821(PON1) 102879084 102879651
LAV: 100667197(PON2) 100675274(PON3) 100675554(PON1)
TMU: 101344330 101360527 101360792
MDO: 100017970(PON2) 100018559(PON3) 100028798
SHR: 100922843 100929514 105750837
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
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)
NPR: 108790495 108790498 108790499
DRE: 335176(pon2) 554122(pon3.1) 568655(pon3.2)
SRX: 107714733 107714734 107723437
SANH: 107657594 107657661 107699523 107699524
SGH: 107570834 107595282 107595292
CCAR: 109074161 109074777
IPU: 108271509
AMEX: 103046166
TRU: 101062836
TNG: GSTEN00034170G001 GSTEN00034171G001
LCO: 104925500 104925501
NCC: 104965579 104965581
MZE: 101475101 101475704
OLA: 101174858 101175104
XMA: 102228189 102233391
PRET: 103478535 103478537
NFU: 107378667 107378669
CSEM: 103388494
LCF: 108891018 108891027
HCQ: 109517591 109517598
BPEC: 110166446 110171411
SASA: 100196477(pon2) 106573659 106598067 106598982 106605980
ELS: 105018843 105018844
SFM: 108940718
LCM: 102361851
CMK: 103176917
BFO: BRAFLDRAFT_100225 BRAFLDRAFT_118130 BRAFLDRAFT_208249 BRAFLDRAFT_221411 BRAFLDRAFT_225661 BRAFLDRAFT_237432 BRAFLDRAFT_260864
SPU: 100889706 582780 752021
APLC: 110985577 110985825 110988044
SKO: 100378655 102801568 102809273
NAI: NECAME_03451
LOA: LOAG_02638
HRO: HELRODRAFT_97933
LGI: LOTGIDRAFT_174719
CRG: 105322421 105340244 105346951
MYI: 110446029 110446051 110450177 110450178 110460254
OBI: 106873488
LAK: 106158780 106181365
NVE: NEMVE_v1g112795
EPA: 110240777 110240778 110246487
ADF: 107327691 107348033
HMG: 100211341
AQU: 105316431
YLI: YALI0C00110g YALI0C21516g
SSCK: SPSK_02462
PBL: PAAG_03299
PBN: PADG_03170
ADL: AURDEDRAFT_104672
GTR: GLOTRDRAFT_93268
SCM: SCHCODRAFT_28591
WSE: WALSEDRAFT_62365 WALSEDRAFT_70483
PGR: PGTG_01500
MLR: MELLADRAFT_91179
SRE: PTSG_06241
TET: TTHERM_000470733
OSG: BST96_17895
PSPI: PS2015_622
MSD: MYSTI_07768
RBS: RHODOSMS8_00093
 » 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

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