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ENZYME

ENZYME entry: EC 3.1.1.2

PURL: https://purl.expasy.org/enzyme/EC/3.1.1.2
Accepted Name
arylesterase
Alternative Name(s)
A-esterase
paraoxonase
Reaction catalysed
a phenyl acetate + H2O = a phenol + acetate + H(+)
Comment(s)
  • Acts on many phenolic esters.
  • It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases.
  • The natural substrates of the paraoxonases are lactones, with (+-)-5- hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate.
Cross-references
BRENDA3.1.1.2
EC2PDB3.1.1.2
ExplorEnz3.1.1.2
KEGG Ligand Database for Enzyme Nomenclature3.1.1.2
IUBMB Enzyme Nomenclature3.1.1.2
MEDLINEFind literature relating to 3.1.1.2
MetaCyc3.1.1.2
Rhea expert-curated reactions3.1.1.2
UniProtKB/Swiss-Prot
B5BLW5, ARE_SACSOP22862, ESTE_PSEFLQ07792, ESTE_VIBMI
P27169, PON1_HUMANP52430, PON1_MOUSEP27170, PON1_RABIT
P55159, PON1_RATQ58DS7, PON2_BOVINP54832, PON2_CANLF
Q90952, PON2_CHICKQ15165, PON2_HUMANQ91090, PON2_MELGA
Q62086, PON2_MOUSEQ6AXM8, PON2_RATQ15166, PON3_HUMAN
Q62087, PON3_MOUSEQ9BGN0, PON3_RABITQ68FP2, PON3_RAT
P0ADA2, TESA_ECOL6P0ADA1, TESA_ECOLI

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-