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Literature summary for 1.11.1.5 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)

Cloned (Comment) Organism
-
Saccharomyces cerevisiae

Protein Variants

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Synonyms

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