Pub. Date : 2007 Oct
PMID : 17693598
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Dal5p has been shown previously to act as an allantoate/ureidosuccinate permease and to play a role in the utilization of certain dipeptides as a nitrogen source in Saccharomyces cerevisiae. | Dipeptides | allantoate permease | Saccharomyces cerevisiae S288C |
| 2 | Here, we provide direct evidence that dipeptides are transported by Dal5p, although the affinity of Dal5p for allantoate and ureidosuccinate is higher than that for dipeptides. | Dipeptides | allantoate permease | Saccharomyces cerevisiae S288C |
| 3 | Here, we provide direct evidence that dipeptides are transported by Dal5p, although the affinity of Dal5p for allantoate and ureidosuccinate is higher than that for dipeptides. | Dipeptides | allantoate permease | Saccharomyces cerevisiae S288C |
| 4 | Here, we provide direct evidence that dipeptides are transported by Dal5p, although the affinity of Dal5p for allantoate and ureidosuccinate is higher than that for dipeptides. | Dipeptides | allantoate permease | Saccharomyces cerevisiae S288C |
| 5 | In contrast to the well-studied di/tripeptide transporter Ptr2p, whose substrate specificity is very broad, Dal5p preferred to transport non-N-end rule dipeptides. | Dipeptides | allantoate permease | Saccharomyces cerevisiae S288C |
| 6 | Toxic dipeptide and uptake assays indicated that either Ptr2p or Dal5p was predominantly used for dipeptide transport in the common laboratory strains S288c and W303, respectively. | Dipeptides | allantoate permease | Saccharomyces cerevisiae S288C |
| 7 | Toxic dipeptide and uptake assays indicated that either Ptr2p or Dal5p was predominantly used for dipeptide transport in the common laboratory strains S288c and W303, respectively. | Dipeptides | allantoate permease | Saccharomyces cerevisiae S288C |