CATH Classification

Domain Context

CATH Clusters

Superfamily Creatinase/prolidase N-terminal domain
Functional Family

Enzyme Information

3.1.8.1
Aryldialkylphosphatase.
based on mapping to UniProt Q44238
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.
3.4.13.9
Xaa-Pro dipeptidase.
based on mapping to UniProt Q44238
Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
-!- Possibly thiol dependent. -!- Cytosolic from most animal tissues. -!- Belongs to peptidase family M24A. -!- Formerly EC 3.4.3.7.
3.1.8.2
Diisopropyl-fluorophosphatase.
based on mapping to UniProt Q44238
Diisopropyl fluorophosphate + H(2)O = diisopropyl phosphate + fluoride.
-!- Acts on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including nerve gases). -!- Inhibited by chelating agents. -!- Related to EC 3.1.8.1. -!- Formerly EC 3.8.2.1.

UniProtKB Entries (1)

Q44238
PEPQ_ALTSX
Alteromonas sp.
Xaa-Pro dipeptidase

PDB Structure

PDB 3L7G
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase.
Vyas, N.K., Nickitenko, A., Rastogi, V.K., Shah, S.S., Quiocho, F.A.
Biochemistry