Human renin inhibition by a diazoacyl reagent: Relationship of the enzyme to other proteinases

摘要: Abstract Human renin is inactivated by a diazoacyl compound (diazoacetylglycine ethyl ester; N 2 CHCO-Gly-OEt) in the presence of Cu(II). The mechanism inactivation presumably identical to that which has been determined for pepsin and several other proteinases: esterification β-carboxyl an aspartic acid residue at active site enzyme. Renin's inhibition reagent, its specificity toward hydrophobic sequence, pepstatin, all suggest close relationship proteinases, especially cathepsin D. However, renin, neutral proteinase, would be better classified together with diazoacyl-inhibited enzymes rather than pH optimum. term “aspartic proteinase” suggested this group enzymes.