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:C00548];
H2O [CPD:C00001]
Product
phenol [CPD:C00146];
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: 
101146649(PON1) 101147009(PON3) 101147360(PON2)
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: 
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)
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)
SSC: 
CFR: 
102519221(PON3) 102519463(PON1) 102521631(PON2)
ECB: 
100051896(PON1) 100051959(PON3) 100062686(PON2)
MYB: 
102249558(PON3) 102250151(PON1) 102251833(PON2)
MDO: 
SHR: 
100929514(PON3)
GGA: 
395830(PON2)
MGP: 
100303695(PON2)
TGU: 
100218152(PON2)
FAB: 
101812552(PON2)
PHI: 
102101075(PON2)
APLA: 
101800414(PON2)
FPG: 
101913744(PON2)
FCH: 
102055053(PON2)
CLV: 
102089494(PON2)
ASN: 
102370400(PON2)
PSS: 
102457846(PON2)
ACS: 
XLA: 
XTR: 
448598(pon2)
DRE: 
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
BFO: 
SPU: 
LOA: 
NVE: 
HMG: 
YLI: 
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.
  Organism
Rattus norvegicus [GN:rno], Equus caballus [GN:ecb], Oryctolagus cuniculus
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.
  Organism
Sus scofa [GN:ssc]
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.
  Organism
Cavia porcellus
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.
  Organism
Rattus norvegicus [GN:rno]
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.
  Organism
Homo sapiens [GN:hsa], Mus musculus [GN:mmu], Bos taurus [GN:bta], Sus scofa [GN:ssc], Felis catus, Capra hircus, Oryctolagus cuniculus, Ovis aries
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.
  Organism
Homo sapiens [GN:hsa], Mus musculus [GN:mmu], Rattus norvegicus [GN:rno], Oryctolagus cuniculus
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.
  Organism
Homo sapiens [GN:hsa]
  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

DBGET integrated database retrieval system