Expasy logo

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
Rhea expert-curated reactions3.1.1.2
ExplorEnz3.1.1.2
IUBMB Enzyme Nomenclature3.1.1.2
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
BRENDA3.1.1.2
MetaCyc3.1.1.2
KEGG Ligand Database for Enzyme Nomenclature3.1.1.2
EC2PDB3.1.1.2
MEDLINEFind literature relating to 3.1.1.2

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.-.-.-