Pub. Date : 2012 Nov 23
PMID : 23043141
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | BACKGROUND: Succinate dehydrogenase (SDH) requires a covalent addition of FAD for catalytic function. | Flavin-Adenine Dinucleotide | succinate dehydrogenase complex iron sulfur subunit B | Homo sapiens |
| 2 | BACKGROUND: Succinate dehydrogenase (SDH) requires a covalent addition of FAD for catalytic function. | Flavin-Adenine Dinucleotide | succinate dehydrogenase complex iron sulfur subunit B | Homo sapiens |
| 3 | CONCLUSION: SDH assembly is dependent on FAD binding to Sdh1 but not covalent binding. | Flavin-Adenine Dinucleotide | succinate dehydrogenase complex iron sulfur subunit B | Homo sapiens |
| 4 | CONCLUSION: SDH assembly is dependent on FAD binding to Sdh1 but not covalent binding. | Flavin-Adenine Dinucleotide | succinate dehydrogenase complex iron sulfur subunit B | Homo sapiens |
| 5 | The enzymatic function of succinate dehydrogenase (SDH) is dependent on covalent attachment of FAD on the ~70-kDa flavoprotein subunit Sdh1. | Flavin-Adenine Dinucleotide | succinate dehydrogenase complex iron sulfur subunit B | Homo sapiens |
| 6 | The enzymatic function of succinate dehydrogenase (SDH) is dependent on covalent attachment of FAD on the ~70-kDa flavoprotein subunit Sdh1. | Flavin-Adenine Dinucleotide | succinate dehydrogenase complex iron sulfur subunit B | Homo sapiens |
| 7 | The enzymatic function of succinate dehydrogenase (SDH) is dependent on covalent attachment of FAD on the ~70-kDa flavoprotein subunit Sdh1. | Flavin-Adenine Dinucleotide | succinate dehydrogenase complex iron sulfur subunit B | Homo sapiens |