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Literature summary for 3.4.23.15 extracted from

  • Nakagawa, T.; Akaki, J.; Satou, R.; Takaya, M.; Iwata, H.; Katsurada, A.; Nishiuchi, K.; Ohmura, Y.; Suzuki, F.; Nakamura, Y.
    The His-Pro-Phe motif of angiotensinogen is a crucial determinant of the substrate specificity of renin (2007), Biol. Chem., 388, 237-246.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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 recombinant
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
angiotensinogen + H2O the His-Pro-Phe motif of angiotensinogen is a crucial determinant of the substrate specificity of renin. Mutant angiotensinogens in which the Ile-His-Pro-Phe-His-Leu sequence at positions 5-10 of wild-type angiotensinogen is replaced by either His-Pro-Phe-His-Leu-Leu or Ala-Ile-His-Pro-Phe-His are cleaved by renin at the C-terminal side of residues 9 and 11, respectively, while wild-type angiotensinogen is cleaved at residue 10. A triple Ala substitution for the His-Pro-Phe motif of angiotensinogen prevents its cleavage by renin. In contrast, triple Ala substitution for residues 9-11, including the natural site of cleavage by renin, allows cleavage between the two Ala residues at positions 10 and 11 Homo sapiens angiotensin I + angiotensinogen propeptide
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 ?
megsin + H2O the protein which carries a naturally occurring His-Pro-Phe sequence, is cleaved by renin at the C-terminal side of the His-Pro-Phe-Leu-Phe sequence Homo sapiens ?
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 ?