Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.18 extracted from

  • Seifried, A.; Bergeron, A.; Boivin, B.; Gohla, A.
    Reversible oxidation controls the activity and oligomeric state of the mammalian phosphoglycolate phosphatase AUM (2016), Free Radic. Biol. Med., 97, 75-84 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol
-
Mus musculus
tris(2-carboxyethyl)phosphine
-
Mus musculus

Crystallization (Commentary)

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

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

Inhibitors Comment Organism Structure
H2O2 reversible Mus musculus

KM Value [mM]

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

Organism UniProt Comment Textmining
Mus musculus Q8CHP8 cf. EC 3.1.3.48
-

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
AUM
-
Mus musculus
Pgp
-
Mus musculus

Turnover Number [1/s]

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 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

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