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Literature summary for 1.11.1.11 extracted from

  • Yadav, R.K.; Dolai, S.; Pal, S.; Adak, S.
    Role of tryptophan-208 residue in cytochrome c oxidation by ascorbate peroxidase from Leishmania major-kinetic studies on Trp208Phe mutant and wild type enzyme (2008), Biochim. Biophys. Acta, 1784, 863-871.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
W208F the optical spectrum of the W208F mutant closely resembles that of wild type LmAPX at pH 7.5 in the absence of ascorbate. W208F mutant causes a spectral red shift from high spin to low spin, indicating that the mutant can react with H2O2. Cytochrome c binding affinity to the enzyme does not alter after mutation. The mutant is 1000times less active than the wild type in cytochrome c oxidation Leishmania major
W208Y mutant shows low spin hem. The mutant does not react with H2O2 Leishmania major

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
guaiacol 25°C, mutant enzyme W208F Leishmania major
0.025
-
cytochrome c 25°C, mutant enzyme W208F Leishmania major
6
-
cytochrome c 25°C, wild-type enzyme Leishmania major
6.7
-
guaiacol 25°C, wild-type enzyme Leishmania major

Organism

Organism UniProt Comment Textmining
Leishmania major
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzyme W208F expressed in Escherichia coli Leishmania major

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Cytochrome c + H2O
-
Leishmania major ?
-
?
guaiacol + H2O2
-
Leishmania major ?
-
?
L-ascorbate + H2O2
-
Leishmania major dehydroascorbate + H2O
-
?

Synonyms

Synonyms Comment Organism
LmAPX
-
Leishmania major

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.53
-
ascorbate 25°C, wild-type enzyme Leishmania major
1.83
-
cytochrome c 25°C, wild-type enzyme Leishmania major
2.5
-
guaiacol 25°C, wild-type enzyme Leishmania major