[Zinc-dependent angiotensin-converting enzyme in reactions with various enzymes].
The effects of Zn2+ on the activity of the angiotensin-converting enzyme from bovine lung towards the substrates, FA-Phe-Gly-Gly and Cbz-Phe-His-Leu, have been studied. At pH below 7.0 zinc ions added to the reaction mixture increase the enzyme activity; this stimulating effect is changed to inhibition with a further rise in Zn2+ concentration. It was shown that the dissociation constant for the enzyme--Zn2+ complex and the "optimal" concentrations of Zn2+ needed for the manifestation of the maximal enzymatic activity depend on the nature of the substrate at all pH values studied.
Kost
O A
OA
Sharafutdinov
T Z
TZ
Kazinskaia
N F
NF
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors; D000818:Animals; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D066298:In Vitro Techniques; D007700:Kinetics; D008168:Lung / Q000201:enzymology; D008969:Molecular Sequence Data; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D013379:Substrate Specificity; D015032:Zinc / Q000494:pharmacology*
D000806:Angiotensin-Converting Enzyme Inhibitors; D007703:Peptidyl-Dipeptidase A; D015032:Zinc
Tsinkzavisimyĭ angiotenzin-prevrashchaiushchiĭ ferment v reaktsiiakh s raznymi substratami.