Pub. Date : 1988 Aug 23
PMID : 2851317
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 2 | Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation. | Phenylalanine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 3 | On the basis of X-ray structural information, it was previously proposed that tryptophan-191 of yeast cytochrome c peroxidase (CCP) may be important in determining the spectroscopic and catalytic properties of the enzyme [Edwards, S. L., Xuong, Ng. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 4 | On the basis of X-ray structural information, it was previously proposed that tryptophan-191 of yeast cytochrome c peroxidase (CCP) may be important in determining the spectroscopic and catalytic properties of the enzyme [Edwards, S. L., Xuong, Ng. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 5 | By use of site-directed mutagenesis and an Escherichia coli expression system, a mutant phenylalanine-191 (F191) CCP was prepared in order to examine the effects of altering the H-bonding and pi-pi interactions that occur between Trp-191 and the iron-coordinated proximal His-175 in the parent enzyme. | Phenylalanine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |