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Literature summary extracted from

  • Lee, Y.; Boycheva, S.; Brittain, T.; Boyd, P.D.
    Intramolecular electron transfer in the dihaem cytochrome c peroxidase of Pseudomonas aeruginosa (2007), Chembiochem, 8, 1440-1446.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.5 expression in Escherichia coli Pseudomonas aeruginosa
1.11.1.5 mutants expressed in Escherichia coli Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.5 H71G about 55% of wild-type activity. Five-coordinate, peroxidatic heme structure contrary to six-coordinate structure of wild-type, formation of a tryptophan radical species during catalysis Pseudomonas aeruginosa
1.11.1.5 H71G 55% activity compared to the wild type enzyme, contains a high-spin, presumably five-coordinate, peroxidatic heme site Pseudomonas aeruginosa
1.11.1.5 H71G/W94A about 4% of wild-type activity. Five-coordinate, peroxidatic heme structure contrary to six-coordinate structure of wild-type, formation of a porphyrin radical species during catalysis Pseudomonas aeruginosa
1.11.1.5 H71G/W94A 4% activity compared to the wild type enzyme, contains a high-spin, presumably five-coordinate, peroxidatic heme site Pseudomonas aeruginosa
1.11.1.5 W94A less than 1% of wild-type activity. Six-coordinate heme structure similar to wild-type Pseudomonas aeruginosa
1.11.1.5 W94A less than 1% activity compared to the wild type enzyme, the mutant retains the normal six-coordinate heme structures Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.5 Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.5 ferrocytochrome c + H2O2
-
 Pseudomonas aeruginosa ferricytochrome c + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.5 cytochrome c peroxidase
-
 Pseudomonas aeruginosa