Novel substrates for angiotensin I converting enzyme

Louis B. Hersh; John T. Gafford; James C. Powers; Takumi Tanaka; Ervin G. Erdös

doi:10.1016/0006-291X(83)91199-3

Novel substrates for angiotensin I converting enzyme

Louis B. Hersh, John T. Gafford, James C. Powers, Takumi Tanaka, Ervin G. Erdös

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

Homogenous human angiotensin converting enzyme (EC 3.4.15.1) cleaves dipeptides from the C-terminus of substrates containing a free carboxyl group. In this study we demonstrate that peptides containing a C-terminal nitrobenzylamine are also cleaved by the enzyme. The hydrolysis of these substrates is inhibited by the specific converting enzyme inhibitors captopril and MK421 as well as by anti-converting enzyme antibody. Sodium chloride accelerates the rate of hydrolysis forty-fold. The product of the reaction, an amino acid nitrobenzylamide, was identified by thin layer chromatography and high performance liquid chromatography. These results suggest that the carboxyl group is not an absolute requirement for substrate hydrolysis.

Original language	English
Pages (from-to)	654-659
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	110
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(83)91199-3
State	Published - Jan 27 1983

Bibliographical note

Funding Information:
in part by grants from NIH, HL 16320, HL NIDA, DA 02243, and the Robert A. Welch We are grateful for the skilled assistance for the advice and help of Dr. Skidgel

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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Cite this

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title = "Novel substrates for angiotensin I converting enzyme",

abstract = "Homogenous human angiotensin converting enzyme (EC 3.4.15.1) cleaves dipeptides from the C-terminus of substrates containing a free carboxyl group. In this study we demonstrate that peptides containing a C-terminal nitrobenzylamine are also cleaved by the enzyme. The hydrolysis of these substrates is inhibited by the specific converting enzyme inhibitors captopril and MK421 as well as by anti-converting enzyme antibody. Sodium chloride accelerates the rate of hydrolysis forty-fold. The product of the reaction, an amino acid nitrobenzylamide, was identified by thin layer chromatography and high performance liquid chromatography. These results suggest that the carboxyl group is not an absolute requirement for substrate hydrolysis.",

author = "Hersh, {Louis B.} and Gafford, {John T.} and Powers, {James C.} and Takumi Tanaka and Erd{\"o}s, {Ervin G.}",

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T1 - Novel substrates for angiotensin I converting enzyme

AU - Hersh, Louis B.

AU - Gafford, John T.

AU - Powers, James C.

AU - Tanaka, Takumi

AU - Erdös, Ervin G.

N1 - Funding Information: in part by grants from NIH, HL 16320, HL NIDA, DA 02243, and the Robert A. Welch We are grateful for the skilled assistance for the advice and help of Dr. Skidgel

PY - 1983/1/27

Y1 - 1983/1/27

N2 - Homogenous human angiotensin converting enzyme (EC 3.4.15.1) cleaves dipeptides from the C-terminus of substrates containing a free carboxyl group. In this study we demonstrate that peptides containing a C-terminal nitrobenzylamine are also cleaved by the enzyme. The hydrolysis of these substrates is inhibited by the specific converting enzyme inhibitors captopril and MK421 as well as by anti-converting enzyme antibody. Sodium chloride accelerates the rate of hydrolysis forty-fold. The product of the reaction, an amino acid nitrobenzylamide, was identified by thin layer chromatography and high performance liquid chromatography. These results suggest that the carboxyl group is not an absolute requirement for substrate hydrolysis.

AB - Homogenous human angiotensin converting enzyme (EC 3.4.15.1) cleaves dipeptides from the C-terminus of substrates containing a free carboxyl group. In this study we demonstrate that peptides containing a C-terminal nitrobenzylamine are also cleaved by the enzyme. The hydrolysis of these substrates is inhibited by the specific converting enzyme inhibitors captopril and MK421 as well as by anti-converting enzyme antibody. Sodium chloride accelerates the rate of hydrolysis forty-fold. The product of the reaction, an amino acid nitrobenzylamide, was identified by thin layer chromatography and high performance liquid chromatography. These results suggest that the carboxyl group is not an absolute requirement for substrate hydrolysis.

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Novel substrates for angiotensin I converting enzyme

Abstract

Bibliographical note

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