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Literature summary for 1.8.3.1 extracted from

  • Feng, C.; Wilson, H.L.; Hurley, J.K.; Hazzard, J.T.; Tollin, G.; Rajagopalan, K.V.; Enemark, J.H.
    Essential role of conserved arginine 160 in intramolecular electron transfer in human sulfite oxidase (2003), Biochemistry, 42, 12235-12242.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
R160K the intramolecular electron transfer rate constant for the mutant enzyme is about one-fourth that of the wild-type enzyme Homo sapiens
R160Q the intramolecular electron transfer rate constant for the mutant enzyme at pH 6.0 is decreased by nearly 3 orders of magnitude relative to wild-type enzyme. The intramolecular electron transfer is rate-limiting in the catalytic cycle of the mutant, fatal impact of this mutation in patients with this genetic disorder Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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