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Literature summary for 1.11.1.5 extracted from

  • Bidwai, A.; Ayala, C.; Vitello, L.B.; Erman, J.E.
    Apolar distal pocket mutants of yeast cytochrome c peroxidase Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to the triAla, triVal, and triLeu variants (2015), Biochim. Biophys. Acta, 1854, 919-929 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.5

Cloned(Commentary)

Cloned (Comment) Organism
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 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
R48A/W51A/H52A less than 0.02% of wild-type activity. The imidazole binding curve is biphasic. The fast phase of imidazole binding is linearly dependent on the imidazole concentration while the slow phase is independent of imidazole concentration. Imidazole binding is pH dependent with the strongest binding observed at high pH. Mutant displays higher binding affinities for 1-methylimidazole and 4-nitroimidazole than wild-type CcP Saccharomyces cerevisiae
R48L/W51L/H52L less than 0.02% of wild-type activity. The imidazole binding curve is biphasic. The fast phase of imidazole binding is linearly dependent on the imidazole concentration while the slow phase is independent of imidazole concentration. Imidazole binding is pH dependent with the strongest binding observed at high pH. Mutant displays higher binding affinities for 1-methylimidazole and 4-nitroimidazole than wild-type CcP Saccharomyces cerevisiae
R48V/W51V/H52V less than 0.02% of wild-type activity. The imidazole binding curve is biphasic. Both phases have a hyperbolic dependence on the imidazole concentration. Imidazole binding is pH dependent with the strongest binding observed at high pH. Mutant displays higher binding affinities for 1-methylimidazole and 4-nitroimidazole than wild-type CcP Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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