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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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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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container_issue	1
container_start_page	57
container_title	Journal of biochemistry (Tokyo)
container_volume	81
creator	OSHIMA, Genichiro NAGASAWA, Kinzo
description	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.
doi_str_mv	10.1093/oxfordjournals.jbchem.a131450
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School of pharmaceutical Sciences</creatorcontrib><title>Some enzymatic properties of peptidyl dipeptide hydrolase (Angiotensin I-converting enzyme)</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>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. 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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
title	Some enzymatic properties of peptidyl dipeptide hydrolase (Angiotensin I-converting enzyme)
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