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CATH Superfamily 3.40.50.1820

Alpha/Beta hydrolase fold, catalytic domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
alpha/beta hydrolase
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 609: Arylesterase

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Aryldialkylphosphatase. [EC: 3.1.8.1]
An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.
  • Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids.
  • Inhibited by chelating agents.
  • Previously regarded as identical with EC 3.1.1.2.
 25 A0A0U3H9T8 A0A0U3H9T8 A0A0U3H9T8 A0A0U3H9T8 A0A0U3H9T8 B5BLW5 B5BLW5 B5BLW5 B5BLW5 B5BLW5
(15 more...)
Arylesterase. [EC: 3.1.1.2]
A phenyl acetate + H(2)O = a phenol + acetate.
  • 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.
 25 A0A0U3H9T8 A0A0U3H9T8 A0A0U3H9T8 A0A0U3H9T8 A0A0U3H9T8 B5BLW5 B5BLW5 B5BLW5 B5BLW5 B5BLW5
(15 more...)