Prolyl endopeptidase

Sherwin Wilk

doi:10.1016/0024-3205(83)90285-0

Prolyl endopeptidase

Sherwin Wilk

Research output: Contribution to journal › Review article › peer-review

240 Scopus citations

Abstract

Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormonereleasing hormone, thyrotropin releasing hormone, bradykinin and angiotensin II. The structure of β-neo-endorphin suggests that this opioid peptide is formed by the action of prolyl endopeptidase on a precursor of higher molecular weight. Formation of two biologically active fragments of substance P also requires the action of this enzyme. This review summarizes the current knowledge of the biochemistry of this enzyme, and its potential significance for neuropeptide physiology and pharmacology.

Original language	English
Pages (from-to)	2149-2157
Number of pages	9
Journal	Life Sciences
Volume	33
Issue number	22
DOIs	https://doi.org/10.1016/0024-3205(83)90285-0
State	Published - 28 Nov 1983
Externally published	Yes

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@article{5ff6f16e068d49dd9494ce3aec1ed01b,

title = "Prolyl endopeptidase",

abstract = "Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormonereleasing hormone, thyrotropin releasing hormone, bradykinin and angiotensin II. The structure of β-neo-endorphin suggests that this opioid peptide is formed by the action of prolyl endopeptidase on a precursor of higher molecular weight. Formation of two biologically active fragments of substance P also requires the action of this enzyme. This review summarizes the current knowledge of the biochemistry of this enzyme, and its potential significance for neuropeptide physiology and pharmacology.",

author = "Sherwin Wilk",

note = "Funding Information: I thankD r. Marian Orlowski for reviewingt he manuscripta nd for helpful suggestions. Studies from this laboratory were supported by a Research Scientist DevelopmenAt wardM H-OO350a nd an NIH grant (NS-17392).",

year = "1983",

month = nov,

day = "28",

doi = "10.1016/0024-3205(83)90285-0",

language = "English",

volume = "33",

pages = "2149--2157",

journal = "Life Sciences",

issn = "0024-3205",

publisher = "Elsevier Inc.",

number = "22",

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TY - JOUR

T1 - Prolyl endopeptidase

AU - Wilk, Sherwin

N1 - Funding Information: I thankD r. Marian Orlowski for reviewingt he manuscripta nd for helpful suggestions. Studies from this laboratory were supported by a Research Scientist DevelopmenAt wardM H-OO350a nd an NIH grant (NS-17392).

PY - 1983/11/28

Y1 - 1983/11/28

N2 - Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormonereleasing hormone, thyrotropin releasing hormone, bradykinin and angiotensin II. The structure of β-neo-endorphin suggests that this opioid peptide is formed by the action of prolyl endopeptidase on a precursor of higher molecular weight. Formation of two biologically active fragments of substance P also requires the action of this enzyme. This review summarizes the current knowledge of the biochemistry of this enzyme, and its potential significance for neuropeptide physiology and pharmacology.

AB - Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormonereleasing hormone, thyrotropin releasing hormone, bradykinin and angiotensin II. The structure of β-neo-endorphin suggests that this opioid peptide is formed by the action of prolyl endopeptidase on a precursor of higher molecular weight. Formation of two biologically active fragments of substance P also requires the action of this enzyme. This review summarizes the current knowledge of the biochemistry of this enzyme, and its potential significance for neuropeptide physiology and pharmacology.

UR - https://www.scopus.com/pages/publications/0021084784

U2 - 10.1016/0024-3205(83)90285-0

DO - 10.1016/0024-3205(83)90285-0

M3 - Review article

C2 - 6358755

AN - SCOPUS:0021084784

SN - 0024-3205

VL - 33

SP - 2149

EP - 2157

JO - Life Sciences

JF - Life Sciences

IS - 22

ER -

Prolyl endopeptidase

Abstract

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