ENZYME entry: EC 3.1.1.2

Accepted Name
Arylesterase.
Alternative Name(s)
A-esterase.
Paraoxonase.
Reaction catalysed
A phenyl acetate + H(2)O <=> a phenol + acetate
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
PRIAM enzyme-specific profiles3.1.1.2
KEGG Ligand Database for Enzyme Nomenclature3.1.1.2
IUBMB Enzyme Nomenclature3.1.1.2
IntEnz3.1.1.2
MEDLINEFind literature relating to 3.1.1.2
MetaCyc3.1.1.2
UniProtKB/Swiss-Prot
P22862, ESTE_PSEFL;  Q07792, ESTE_VIBMI;  P27169, PON1_HUMAN;  
P52430, PON1_MOUSE;  P27170, PON1_RABIT;  P55159, PON1_RAT;  
Q58DS7, PON2_BOVIN;  P54832, PON2_CANFA;  Q90952, PON2_CHICK;  
Q15165, PON2_HUMAN;  Q91090, PON2_MELGA;  Q62086, PON2_MOUSE;  
Q6AXM8, PON2_RAT;  Q15166, PON3_HUMAN;  Q62087, PON3_MOUSE;  
Q9BGN0, PON3_RABIT;  Q68FP2, PON3_RAT;  

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
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.-.-.-