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Literature summary for 3.4.11.10 extracted from

  • Chu, L.; Lai, Y.; Xu, X.; Eddy, S.; Yang, S.; Song, L.; Kolodrubetz, D.
    A 52-kDa leucyl aminopeptidase from Treponema denticola is a cysteinylglycinase that mediates the second step of glutathione metabolism (2008), J. Biol. Chem., 283, 19351-19358.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Treponema denticola

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 22% residual activity in the presence of 2.0 mM Ca2+ Treponema denticola
EDTA 2% residual activity in the presence of 0.2 mM EDTA Treponema denticola
Zn2+ 23% residual activity in the presence of 2.0 mM Zn2+ Treponema denticola

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.39
-
Cys-Gly recombinant enzyme, at pH 8.0 Treponema denticola
0.44
-
Cys-Gly recombinant enzyme, at pH 7.3 Treponema denticola
0.48
-
Cys-Gly native enzyme, at pH 7.3 Treponema denticola
1.72
-
L-Leu-p-nitroanilide recombinant enzyme, at pH 7.3 Treponema denticola
1.79
-
L-Leu-p-nitroanilide recombinant enzyme, at pH 8.0 Treponema denticola

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 580% relative activity in the presence of 2.0 mM Co2+ Treponema denticola
Mg2+ 258% relative activity in the presence of 2.0 mM Mg2+ Treponema denticola
Mn2+ 510% relative activity in the presence of 2.0 mM Mn2+ Treponema denticola
additional information not stimulated by Zn2+ or Ca2+ Treponema denticola

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
SDS-PAGE Treponema denticola

Organism

Organism UniProt Comment Textmining
Treponema denticola
-
strain ATCC 35404
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, ultrafiltration, and Sepharose Q column chromatography Treponema denticola

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Cys-Gly + H2O preferred substrate Treponema denticola L-Cys + Gly
-
?
glutathione + H2O the enzyme is involved in turnover of glutathione Treponema denticola ?
-
?
L-Leu-p-nitroanilide + H2O
-
Treponema denticola L-Leu + p-nitroaniline
-
?
additional information no activity towards Asp-Gly, Glu-Cys-Gly, and L-Cys Treponema denticola ?
-
?

Synonyms

Synonyms Comment Organism
CGase the protein is a member of the family of metalloproteases called M17 leucine aminopeptidases Treponema denticola
cysteinylglycinase
-
Treponema denticola
Leucyl aminopeptidase
-
Treponema denticola

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
30
-
L-Leu-p-nitroanilide recombinant enzyme, at pH 7.3 Treponema denticola
41.7
-
L-Leu-p-nitroanilide recombinant enzyme, at pH 8.0 Treponema denticola
43.3
-
Cys-Gly recombinant enzyme, at pH 8.0 Treponema denticola
46.7
-
Cys-Gly native enzyme, at pH 7.3 Treponema denticola
60
-
Cys-Gly recombinant enzyme, at pH 7.3 Treponema denticola

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
the activity of CGase for Cys-Gly is optimum at pH 7.3 Treponema denticola
8
-
the activity of CGase for L-Leu-p-nitroanilide is optimum at pH 8.0 Treponema denticola

pH Stability

pH Stability pH Stability Maximum Comment Organism
7.3 8 the amidolytic activity of the enzyme toward Cys-Gly is maximal at pH 7.3/7.4 and declines fairly rapidly at higher or lower pH conditions, the activity of the enzyme with L-Leu-p-nitroanilide is not as sensitive to increases or decreases in pH Treponema denticola