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Literature summary for 1.11.1.5 extracted from

  • Erman, J.E.; Kilheeney, H.; Bidwai, A.K.; Ayala, C.E.; Vitello, L.B.
    Peroxygenase activity of cytochrome c peroxidase and three apolar distal heme pocket mutants: hydroxylation of 1-methoxynaphthalene (2013), BMC Biochem., 14, 19.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.5

Application

Application Comment Organism
biotechnology cytochrome c peroxidase as a platform to develop specific peroxygenation catalysts Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information construction of three apolar distal heme pocket mutants of CcP with enhanced binding of 1-methoxynaphthalene near the heme and enhanced hydroxylation activity of 1-methoxynaphthalene Saccharomyces cerevisiae
R48A/W51A/H52A site-directed mutagenesis, the mutant shows 34fold higher activity with 1-methoxynaphthalene than the wild-type enzyme. While wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, mutant CcP is inactivated within four cycles of the peroxygenase reaction Saccharomyces cerevisiae
R48L/W51L/H52L site-directed mutagenesis, the mutant shows higher activity with 1-methoxynaphthalene than the wild-type enzyme Saccharomyces cerevisiae
R48V/W51V/H52V site-directed mutagenesis, the mutant shows higher activity with 1-methoxynaphthalene than the wild-type enzyme Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ heme Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Oxidation Stability

Oxidation Stability Organism
while the wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, CcP mutant R48A/W51A/H52A is inactivated within four cycles of the peroxygenase reaction Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-methoxynaphthalene + H2O2
-
 Saccharomyces cerevisiae Russig's blue + 2 H2O
-
 ?

Synonyms

Synonyms Comment Organism
CCP
-
 Saccharomyces cerevisiae
cytochrome c peroxidase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00007
-
 1-methoxynaphthalene pH 7.0, 25°C, wild-type enzyme Saccharomyces cerevisiae
0.0022
-
 1-methoxynaphthalene pH 7.0, 25°C, mutant R48L/W51L/H52L Saccharomyces cerevisiae
0.0023
-
 1-methoxynaphthalene pH 7.0, 25°C, mutant R48V/W51V/H52V Saccharomyces cerevisiae
0.0025
-
 1-methoxynaphthalene pH 7.0, 25°C, mutant R48A/W51A/H52A Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
heme
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction while the wild-type CcP is very stable to oxidative degradation by excess hydrogen peroxide, CcP mutant R48A/W51A/H52A is inactivated within four cycles of the peroxygenase reaction Saccharomyces cerevisiae