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Amino Acid Sequence Homology between Pig Heart Lipoamide Dehydrogenase and Human Erythrocyte Glutathione Reductase
Charles H. Williams, L. David Arscott and Georg E. Schulz
Proceedings of the National Academy of Sciences of the United States of America
Vol. 79, No. 7, [Part 1: Biological Sciences] (Apr. 1, 1982), pp. 2199-2201
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/11595
Page Count: 3
You can always find the topics here!Topics: Dehydrogenases, Amino acids, Erythrocytes, Enzymes, Swine, First appearance datums, Thiols, Biochemistry, Species, Humans
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Extensive amino acid sequence homology has been found between nine tryptic peptides of pig heart lipoamide dehydrogenase [NADH:lipoamide oxidoreductase, EC 184.108.40.206] and the sequence of human erythrocyte glutathione reductase [NAD(P)H:glutathione oxidoreductase, EC 220.127.116.11]. The average homology is 40%. Six lipoamide dehydrogenase peptides are homologous with segments of the two parts of the FAD domain of glutathione reductase, one with the NADPH domain, and two with the interface domain. Thus, the homology extends throughout the molecule.
Proceedings of the National Academy of Sciences of the United States of America © 1982 National Academy of Sciences