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Journal Article

Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase

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Schulz,  Georg E.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.pnas.org/content/pnas/79/7/2199.full.pdf
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https://doi.org/10.1073/pnas.79.7.2199
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Citation

Williams J., C. H., Arscott, D. L., & Schulz, G. E. (1982). Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase. Proceedings of the National Academy of Sciences of the United States of America, 79(7), 2199-2201. doi:10.1073/pnas.79.7.2199.


Cite as: https://hdl.handle.net/21.11116/0000-0005-38E3-C
Abstract
Extensive amino acid sequence homology has been found between nine tryptic peptides of pig heart lipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.6.4.3] and the sequence of human erythrocyte glutathione reductase [NAD(P)H:glutathione oxidoreductase, EC 1.6.4.2]. 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.