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Literature summary for 3.1.3.48 extracted from

  • Mijakovic, I.; Musumeci, L.; Tautz, L.; Petranovic, D.; Edwards, R.A.; Jensen, P.R.; Mustelin, T.; Deutscher, J.; Bottini, N.
    In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE (2005), J. Bacteriol., 187, 3384-3390.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
NaCl activating up to 0.5 M Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
D194A compared to wild-type, 5.4% activity with 4-nitrophenyl phosphate Bacillus subtilis
D3A compared to wild-type, 8% activity with 4-nitrophenyl phosphate Bacillus subtilis
H136A compared to wild-type, 7.7% activity with 4-nitrophenyl phosphate Bacillus subtilis
H196A compared to wild-type, 4.1% activity with 4-nitrophenyl phosphate Bacillus subtilis
H42A compared to wild-type, 6.8% activity with 4-nitrophenyl phosphate Bacillus subtilis
H5A compared to wild-type, 9.5% activity with 4-nitrophenyl phosphate Bacillus subtilis
H7A compared to wild-type, 6.3% activity with 4-nitrophenyl phosphate Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
diphosphate 1 mM, 31% residual activity Bacillus subtilis
NaF 1 mM, 85% residual activity Bacillus subtilis
vanadate competitive, 1 mM, 11% residual activity Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.054
-
KRLIEDNE(pY)TARGQ pH 8.0, presence of 1 mM Mn2+ Bacillus subtilis
0.345
-
4-nitrophenyl phosphate pH 8.0, presence of 1 mM Mn2+ Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ or Mn2+, Zn2+, required Bacillus subtilis
Mn2+ or Cu2+, Zn2+, required, Km-value 0.274 mM Bacillus subtilis
additional information not activating: Mg2+, Ca2+ Bacillus subtilis
Zn2+ or Cu2+, Mn2+, required Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
Bacillus subtilis 4-nitrophenol + phosphate
-
?
KRLIEDNE(pY)TARGQ + H2O phosphopeptide derived from autophosphorylation of mammalian tyrosine kinase Lck Bacillus subtilis KRLIEDNEYTARGQ + phosphate
-
?
additional information no substrate: phosphoeptides RRA(pS)VA, KR(pT)IRR Bacillus subtilis ?
-
?
phosphorylated YwqD protein implicated in UDP-glucuronate synthesis Bacillus subtilis YwqD + phosphate
-
?
phosphorylated YwqF protein implicated in UDP-glucuronate synthesis Bacillus subtilis YwqF + phosphate
-
?

Synonyms

Synonyms Comment Organism
YwqE
-
Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.016
-
KRLIEDNE(pY)TARGQ pH 8.0, presence of 1 mM Mn2+ Bacillus subtilis
0.022
-
4-nitrophenyl phosphate pH 8.0, presence of 1 mM Mn2+ Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9 in presence of Mn2+, Zn2+, activity increases with pH-value. In presence of Cu2+, activity is realtively pH-independent Bacillus subtilis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.014
-
vanadate pH 8.0 Bacillus subtilis