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Literature summary for 3.5.3.1 extracted from

  • Srivastava, A.; Dwivedi, N.; Sau, A.K.
    Role of a disulphide bond in Helicobacter pylori arginase (2010), Biochem. Biophys. Res. Commun., 395, 348-351.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Helicobacter pylori

Protein Variants

Protein Variants Comment Organism
C66A residue involved in disulfide bond. Catalytic turnover and the catalytic efficiency for the mutant proteins similar to the wild-type Helicobacter pylori
C73A residue involved in disulfide bond. Catalytic turnover and the catalytic efficiency for the mutant proteins similar to the wild-type Helicobacter pylori

Inhibitors

Inhibitors Comment Organism Structure
dithiothreitol enzyme depleted of metal and reconstituted with Co2+, complete loss of activiy. Enzyme reconstitued with Mn2+, 20% loss of activity. Loss of catalytic activity in the wild-type protein with dithiothreitol is due to the interaction with Co2+ Helicobacter pylori

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5
-
L-arginine mutant C73A, pH 7.2, 37°C Helicobacter pylori
6
-
L-arginine mutant C66A, pH 7.2, 37°C Helicobacter pylori
6.2
-
L-arginine wild-type, pH 7.2, 37°C Helicobacter pylori

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ enzyme is selective for Co2+ Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine + H2O
-
Helicobacter pylori L-ornithine + urea
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
62
-
melting temperature, mutants C73A and C66A depleted of Co2+ Helicobacter pylori
66
-
melting temperature, mutant C73A Helicobacter pylori
67
-
melting temperature, mutant C66A Helicobacter pylori
69
-
melting temperature, wild-type depleted of Co2+ Helicobacter pylori
71
-
melting temperature, wild-type Helicobacter pylori

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.37
-
L-arginine mutant C66A, pH 7.2, 37°C Helicobacter pylori
0.52
-
L-arginine wild-type, pH 7.2, 37°C Helicobacter pylori
0.53
-
L-arginine mutant C73A, pH 7.2, 37°C Helicobacter pylori

General Information

General Information Comment Organism
metabolism the disulfide bond is important for the overall stability and folding of the protein. Mutant proteins lacking the disulfide bond start to unfold at lower temperature than the wild-type. In the mutant proteins, the Tm of the holoenzyme is 4°C higher than that of the apoenzyme indicating that in the absence of the disulfide bond the metal ions have relatively larger role in the stability of the mutant proteins compared to the wild-type Helicobacter pylori

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.062
-
L-arginine mutant C66A, pH 7.2, 37°C Helicobacter pylori
0.084
-
L-arginine wild-type, pH 7.2, 37°C Helicobacter pylori
0.11
-
L-arginine mutant C73A, pH 7.2, 37°C Helicobacter pylori