PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7826393-0 1995 Glutathione reductase and lipoamide dehydrogenase have opposite stereospecificities for alpha-lipoic acid enantiomers. Thioctic Acid 88-105 glutathione-disulfide reductase Homo sapiens 0-21 7826393-2 1995 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 30-47 glutathione-disulfide reductase Homo sapiens 81-102 7826393-3 1995 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 62-77 glutathione-disulfide reductase Homo sapiens 10-31 7826393-3 1995 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 200-215 glutathione-disulfide reductase Homo sapiens 10-31 7826393-3 1995 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 248-263 glutathione-disulfide reductase Homo sapiens 10-31 7826393-4 1995 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 59-74 glutathione-disulfide reductase Homo sapiens 10-31 7826393-4 1995 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 112-127 glutathione-disulfide reductase Homo sapiens 10-31 7826393-4 1995 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 145-160 glutathione-disulfide reductase Homo sapiens 10-31 7826393-5 1995 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 41-52 glutathione-disulfide reductase Homo sapiens 0-21