Some enzymatic properties of peptidyl dipeptide hydrolase (Angiotensin I-converting enzyme)

Peptidyldipeptide hydrolase [angiotensin I-converting enzyme, EC 3.4.15.1] was inhibited by inorganic and organic phosphorus compounds tested, except for β-glycerophosphate, 5′-AMP, and 5′-ADP, at the reagent concentrations used. Orthophosphate and pyrophosphate nonspecifically inhibited the enzyme...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1977, Vol.81 (1), p.57-63
Main Authors: OSHIMA, Genichiro, NAGASAWA, Kinzo
Format: Article
Language:English
Subjects:
Acetates - pharmacology
Adenine Nucleotides - pharmacology
Angiotensin-Converting Enzyme Inhibitors
Animals
Anions - pharmacology
Benzoates - pharmacology
Carboxylic Acids - pharmacology
Detergents - pharmacology
Kidney - enzymology
Laurates - pharmacology
Phenylpropionates - pharmacology
Phosphates - pharmacology
Swine
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Summary:Peptidyldipeptide hydrolase [angiotensin I-converting enzyme, EC 3.4.15.1] was inhibited by inorganic and organic phosphorus compounds tested, except for β-glycerophosphate, 5′-AMP, and 5′-ADP, at the reagent concentrations used. Orthophosphate and pyrophosphate nonspecifically inhibited the enzyme activity. The enzyme was also inhibited specifically by carboxylates. The degree of inhibition by aliphatic monocarboxylates increased in proportion to their chain length up to C14. Aromatic and ω-phenylalkylcarboxylates also inhibited the enzyme activity. The enzyme was noncom-petitively inhibited by acetate, 3-phenylpropionate and laurate. The K1's for acetate, 3-phenylpropionate, and laurate were 60, 3.3, and 2.5 mM, respectively.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a131450