CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.350 | Creatine Amidinohydrolase; Chain A, domain 1 | |
3.40.350.10 | Creatinase/prolidase N-terminal domain |
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 | 4ZWU |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Engineering the Organophosphorus Acid Anhydrolase Enzyme for Increased Catalytic Efficiency and Broadened Stereospecificity on Russian VX.
Biochemistry
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