Enzyme

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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;

3D structure

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References

External Links

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
MSA:

3.11.1.3;

Phylogenetic Tree:

3.11.1.3;

Uniprot:
M-CSA:
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

References

TitleAuthorsDatePubMed 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 O2006 Sep 2616981709
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 JP2003 Jun 2712697754
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 JP2000 Jan10648102