Pub. Date : 1995 Jan 17
PMID : 7826393
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Glutathione reductase and lipoamide dehydrogenase have opposite stereospecificities for alpha-lipoic acid enantiomers. | Thioctic Acid | glutathione-disulfide reductase | Homo sapiens |
| 2 | Both (R+) and (S-) isomers of alpha-lipoic acid were analyzed as substrates with glutathione reductase from several sources and with mammalian lipoamide dehydrogenase. | Thioctic Acid | glutathione-disulfide reductase | Homo sapiens |
| 3 | Mammalian glutathione reductase catalyzed faster reduction of (S)-lipoic acid (1.4-2.4-fold greater activity) than of (R)-lipoic acid, whereas lipoamide dehydrogenase had a very marked preference for (R)-lipoic acid (18-fold greater activity) over (S)-lipoic acid. | Thioctic Acid | glutathione-disulfide reductase | Homo sapiens |
| 4 | Mammalian glutathione reductase catalyzed faster reduction of (S)-lipoic acid (1.4-2.4-fold greater activity) than of (R)-lipoic acid, whereas lipoamide dehydrogenase had a very marked preference for (R)-lipoic acid (18-fold greater activity) over (S)-lipoic acid. | Thioctic Acid | glutathione-disulfide reductase | Homo sapiens |
| 5 | Mammalian glutathione reductase catalyzed faster reduction of (S)-lipoic acid (1.4-2.4-fold greater activity) than of (R)-lipoic acid, whereas lipoamide dehydrogenase had a very marked preference for (R)-lipoic acid (18-fold greater activity) over (S)-lipoic acid. | Thioctic Acid | glutathione-disulfide reductase | Homo sapiens |
| 6 | Mammalian glutathione reductase showed better affinity for (S)-lipoic acid substrate; Km values were 3.5 mM for (S)-lipoic acid and and 7 mM for (R)-lipoic acid. | Thioctic Acid | glutathione-disulfide reductase | Homo sapiens |
| 7 | Mammalian glutathione reductase showed better affinity for (S)-lipoic acid substrate; Km values were 3.5 mM for (S)-lipoic acid and and 7 mM for (R)-lipoic acid. | Thioctic Acid | glutathione-disulfide reductase | Homo sapiens |
| 8 | Mammalian glutathione reductase showed better affinity for (S)-lipoic acid substrate; Km values were 3.5 mM for (S)-lipoic acid and and 7 mM for (R)-lipoic acid. | Thioctic Acid | glutathione-disulfide reductase | Homo sapiens |
| 9 | Glutathione reductase from yeast reduced lipoic acid less efficiently than the mammalian enymes, had a Km for both stereoisomers of about 10 mM, and showed little stereospecificity. | Thioctic Acid | glutathione-disulfide reductase | Homo sapiens |