Activating Compound | Comment | Organism | Structure |
---|---|---|---|
dithiothreitol | - |
Mus musculus | |
tris(2-carboxyethyl)phosphine | - |
Mus musculus |
Crystallization (Comment) | Organism |
---|---|
protein-ligand interaction analysis. The Cys26 thiol group can engage in a van-der-Waals interaction with Ser58. The reduction-induced conformational change in wild-type is likely triggered by loss of the Cys104/Cys243 disulfide bridge between the PGP core and cap domains | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
C243S | very low stimulation by dithiothreitol | Mus musculus |
C297S | protein displays a complete lack of tetrameric species | Mus musculus |
C35S | very low stimulation by dithiothreitol | Mus musculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
H2O2 | reversible | Mus musculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.3 | - |
2-Phosphoglycolate | pH not specified in the publication, temperature not specified in the publication | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q8CHP8 | cf. EC 3.1.3.48 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-Phosphoglycolate + H2O | - |
Mus musculus | Glycolate + phosphate | - |
? | |
4-nitrophenyl phosphate + H2O | - |
Mus musculus | 4-nitrophenol + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | SEC-multi angle light scattering analysis, the mass fractions show a tetramer/dimer distribution of 13.8/ 84.5% for untreated PGP, and of 6.6/92.5% for the tris(2-carboxyethyl)phosphine-treated enzyme | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
AUM | - |
Mus musculus |
Pgp | - |
Mus musculus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.13 | - |
2-Phosphoglycolate | pH not specified in the publication, temperature not specified in the publication | Mus musculus |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.034 | - |
pH not specified in the publication, temperature not specified in the publication | Mus musculus | H2O2 |
General Information | Comment | Organism |
---|---|---|
metabolism | cysteine residues Cys35, Cys104 and Cys243 in the catalytic core domain of PGP mediate the reversible inhibition of PGP activity and the associated, redox-dependent conformational changes. Cys35 oxidation weakens van-der-Waals interactions with Thr67, a conserved catalytic residue required for substrate coordination. Cys104 and Cys243 form a redox-dependent disulfide bridge between the PGP catalytic core and cap domains. Cys297 in the PGP cap domain is essential for redox-dependent PGP oligomerization, and PGP oxidation/oligomerization occurs in response to stimulation of cells with EGF | Mus musculus |