Pub. Date : 2016 Dec
PMID : 27694803
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification. | Uridine | diphthamide biosynthesis 3 | Homo sapiens |
2 | Diphthamide and the tRNA wobble uridine modifications both require diphthamide biosynthesis 3 (Dph3) protein as an electron donor for the iron-sulfur clusters in their biosynthetic enzymes. | diphthamide | diphthamide biosynthesis 3 | Homo sapiens |
3 | Diphthamide and the tRNA wobble uridine modifications both require diphthamide biosynthesis 3 (Dph3) protein as an electron donor for the iron-sulfur clusters in their biosynthetic enzymes. | Uridine | diphthamide biosynthesis 3 | Homo sapiens |
4 | Diphthamide and the tRNA wobble uridine modifications both require diphthamide biosynthesis 3 (Dph3) protein as an electron donor for the iron-sulfur clusters in their biosynthetic enzymes. | diphthamide | diphthamide biosynthesis 3 | Homo sapiens |
5 | Diphthamide and the tRNA wobble uridine modifications both require diphthamide biosynthesis 3 (Dph3) protein as an electron donor for the iron-sulfur clusters in their biosynthetic enzymes. | Iron | diphthamide biosynthesis 3 | Homo sapiens |
6 | Diphthamide and the tRNA wobble uridine modifications both require diphthamide biosynthesis 3 (Dph3) protein as an electron donor for the iron-sulfur clusters in their biosynthetic enzymes. | Sulfur | diphthamide biosynthesis 3 | Homo sapiens |
7 | Here, using a proteomic approach, we identified Saccharomyces cerevisiae cytochrome b5 reductase (Cbr1) as a NADH-dependent reductase for Dph3. | NAD | diphthamide biosynthesis 3 | Homo sapiens |
8 | The NADH- and Cbr1-dependent reduction of Dph3 may provide a regulatory linkage between cellular metabolic state and protein translation. | NAD | diphthamide biosynthesis 3 | Homo sapiens |