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Literature summary extracted from

  • Pearl, N.M.; Jacobson, T.; Meyen, C.; Clementz, A.G.; Ok, E.Y.; Choi, E.; Wilson, K.; Vitello, L.B.; Erman, J.E.
    Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: evidence for a single, catalytically active, cytochrome c binding domain (2008), Biochemistry, 47, 2766-2775.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.5
-
 Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.5 D34K the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c Saccharomyces cerevisiae
1.11.1.5 D37K the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c Saccharomyces cerevisiae
1.11.1.5 E118K the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c Saccharomyces cerevisiae
1.11.1.5 E290K the mutation causes large increases in the Michaelis constant indicating a reduced affinity for cytochrome c Saccharomyces cerevisiae
1.11.1.5 K149D positive-to-negative charge-reversal mutant Saccharomyces cerevisiae
1.11.1.5 R31E positive-to-negative charge-reversal mutant Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.5 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.5
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.5 ferrocytochrome c + H2O2
-
 Saccharomyces cerevisiae ferricytochrome c + H2O
-
 ?
1.11.1.5 iso-1 ferrocytochrome c + H2O2 C102T Saccharomyces cerevisiae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.5 CCP
-
 Saccharomyces cerevisiae
1.11.1.5 cytochrome c peroxidase
-
 Saccharomyces cerevisiae