[HTML][HTML] Distinct multisite synergistic interactions determine substrate specificities of human chymase and rat chymase-1 for angiotensin II formation and degradation
S Sanker, UM Chandrasekharan, D Wilk… - Journal of Biological …, 1997 - ASBMB
Human chymase and rat chymase-1 are mast cell serine proteases involved in angiotensin II
(Ang II) formation and degradation, respectively. Previous studies indicate that both these
enzymes have similar P 1 and P 2 preferences, which are the major determinants of
specificity. Surprisingly, despite the occurrence of optimal P 2 and P 1 residues at the Phe
8↓ and Tyr 4↓ bonds (where↓, indicates the scissile bond in peptide substrates) in Ang I
(DRVYIHPFHL), human chymase cleaves the Phe 8↓ bond with an∼ 750-fold higher …
(Ang II) formation and degradation, respectively. Previous studies indicate that both these
enzymes have similar P 1 and P 2 preferences, which are the major determinants of
specificity. Surprisingly, despite the occurrence of optimal P 2 and P 1 residues at the Phe
8↓ and Tyr 4↓ bonds (where↓, indicates the scissile bond in peptide substrates) in Ang I
(DRVYIHPFHL), human chymase cleaves the Phe 8↓ bond with an∼ 750-fold higher …