EC Tree |
3. Hydrolases |
3.11 Acting on carbon-phosphorus bonds |
3.11.1 Acting on carbon-phosphorus bonds (only sub-subclass identified to date) |
ID: | 3.11.1.3 |
---|---|
Description: | Phosphonopyruvate hydrolase. |
Alternative Name: |
PPH. |
Cath: | 3.20.20.60; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 3.11.1.3 |
BRENDA Enzyme Link: | BRENDA 3.11.1.3 |
KEGG Enzyme Link: | KEGG3.11.1.3 |
BioCyc Enzyme Link: | BioCyc 3.11.1.3 |
ExPASy Enzyme Link: | ExPASy3.11.1.3 |
EC2PDB Enzyme Link: | EC2PDB 3.11.1.3 |
ExplorEnz Enzyme Link: | ExplorEnz 3.11.1.3 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.11.1.3 |
IntEnz Enzyme Link: | IntEnz 3.11.1.3 |
MEDLINE Enzyme Link: | MEDLINE 3.11.1.3 |
RHEA:16673 | 3-phosphonopyruvate + H2O = H(+) + phosphate + pyruvate |
RULE(radius=1) | [*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[CH2;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[CH3;+0:5].[*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[OH;+0:7] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily. | Chen CC, Han Y, Niu W, Kulakova AN, Howard A, Quinn JP, Dunaway-Mariano D, Herzberg O | 2006 Sep 26 | 16981709 |
The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2. | Kulakova AN, Wisdom GB, Kulakov LA, Quinn JP | 2003 Jun 27 | 12697754 |
Initial in vitro characterisation of phosphonopyruvate hydrolase, a novel phosphate starvation-independent, carbon-phosphorus bond cleavage enzyme in Burkholderia cepacia Pal6. | Ternan NG, Hamilton JT, Quinn JP | 2000 Jan | 10648102 |