Title : Key roles of Arg(5), Tyr(10) and his residues in Aβ-heme peroxidase: relevance to Alzheimer's disease.

Pub. Date : 2014 Sep 26

PMID : 25193696






5 Functional Relationships(s)
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1 Our results indicated that both histidine residues (His(13), His(14)) in Abeta1-16 and free histidine enhanced the peroxidase activity of heme, hence His residues were essential in peroxidase activity of Abeta-heme complexes. Histidine amyloid beta precursor protein Homo sapiens
2 Our results indicated that both histidine residues (His(13), His(14)) in Abeta1-16 and free histidine enhanced the peroxidase activity of heme, hence His residues were essential in peroxidase activity of Abeta-heme complexes. Histidine amyloid beta precursor protein Homo sapiens
3 Our results indicated that both histidine residues (His(13), His(14)) in Abeta1-16 and free histidine enhanced the peroxidase activity of heme, hence His residues were essential in peroxidase activity of Abeta-heme complexes. Histidine amyloid beta precursor protein Homo sapiens
4 Our results indicated that both histidine residues (His(13), His(14)) in Abeta1-16 and free histidine enhanced the peroxidase activity of heme, hence His residues were essential in peroxidase activity of Abeta-heme complexes. Histidine amyloid beta precursor protein Homo sapiens
5 However, three of these residues (Arg(5), Tyr(10) and His(13)) identified in this study are all absent in rodents, where rodent Abeta-heme complex lacks peroxidase activity and it does not show AD, implicating the novel significance of these residues as well as human Abeta-heme peroxidase in the pathology of AD. Histidine amyloid beta precursor protein Homo sapiens