Cleavage of des-Arg9-bradykinin by angiotensin I-converting enzyme from pig kidney cortex.
Fast and very slow hydrolyses of des-Arg9-bradykinin and angiotensin II by angiotensin I-converting enzyme were detected by high performance liquid chromatography. The Michaelis constants of the enzyme, Km values, for des-Arg9-bradykinin and bradykinin were found to be 0.24 mM and 4.4 microM, and the maximum velocities, Vmax values (mumol . min-1 . mg protein-1) for these compounds to be 3.24 and 0.34, respectively. The enzyme also hydrolyzed Z-Gly-Pro-Gly-Gly-Pro-Ala to a tripeptide that was identified as dansyl-Gly-Pro-Ala by TLC on polyamide. These observations show that the enzyme hydrolyzes the peptides at the bond before the prolyl residue in the penultimate position.
Oshima
G
G
Hiraga
Y
Y
Shirono
K
K
Oh-ishi
S
S
Sakakibara
S
S
Kinoshita
T
T
D000804:Angiotensin II / Q000378:metabolism; D000818:Animals; D001920:Bradykinin / Q000031:analogs & derivatives* / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D006868:Hydrolysis; D007672:Kidney Cortex / Q000201:enzymology*; D007700:Kinetics; D009842:Oligopeptides / Q000378:metabolism; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D013379:Substrate Specificity; D013552:Swine
D009842:Oligopeptides; D000804:Angiotensin II; C024626:bradykinin, des-Arg(9)-; D007703:Peptidyl-Dipeptidase A; D001920:Bradykinin