Two forms of prolyl endopeptidase with different activities

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Prolyl endopeptidase, an enzyme exhibiting high specificity towards the Pro-Xaa bond, is thought to play an important role in the metabolism of biologically active peptides. We have purified the enzyme from pig muscle and observed significant differences in its kinetic behavior as compared to the extensively studied serine proteases, such as chymotrypsin. Thus, pH-dependence of, and kinetic deuterium isotope effects on, the rate constants indicated that the enzyme has two forms, which exhibit different activities and interconvert with changing pH. It can be concluded that a general base/acid-catalyzed acylation step is rate-limiting in the lower pH range, and an isotopically stlent step, probably a conformational change preceding the acylation dominates the reaction in the physiological PH range.

Original languageEnglish
Pages (from-to)721-726
Number of pages6
JournalBiomedica Biochimica Acta
Volume50
Issue number4-6
Publication statusPublished - 1991

Fingerprint

prolyl oligopeptidase
Acylation
Enzymes
Kinetics
Deuterium
Chymotrypsin
Serine Proteases
Metabolism
Isotopes
Muscle
Rate constants
Swine
Muscles
Peptides
Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Two forms of prolyl endopeptidase with different activities. / Polgár, L.

In: Biomedica Biochimica Acta, Vol. 50, No. 4-6, 1991, p. 721-726.

Research output: Contribution to journalArticle

@article{f0be76eb930c4354bdd653a649d426ad,
title = "Two forms of prolyl endopeptidase with different activities",
abstract = "Prolyl endopeptidase, an enzyme exhibiting high specificity towards the Pro-Xaa bond, is thought to play an important role in the metabolism of biologically active peptides. We have purified the enzyme from pig muscle and observed significant differences in its kinetic behavior as compared to the extensively studied serine proteases, such as chymotrypsin. Thus, pH-dependence of, and kinetic deuterium isotope effects on, the rate constants indicated that the enzyme has two forms, which exhibit different activities and interconvert with changing pH. It can be concluded that a general base/acid-catalyzed acylation step is rate-limiting in the lower pH range, and an isotopically stlent step, probably a conformational change preceding the acylation dominates the reaction in the physiological PH range.",
author = "L. Polg{\'a}r",
year = "1991",
language = "English",
volume = "50",
pages = "721--726",
journal = "Biomedica Biochimica Acta",
issn = "0232-766X",
publisher = "Akademie Verlag GMBH",
number = "4-6",

}

TY - JOUR

T1 - Two forms of prolyl endopeptidase with different activities

AU - Polgár, L.

PY - 1991

Y1 - 1991

N2 - Prolyl endopeptidase, an enzyme exhibiting high specificity towards the Pro-Xaa bond, is thought to play an important role in the metabolism of biologically active peptides. We have purified the enzyme from pig muscle and observed significant differences in its kinetic behavior as compared to the extensively studied serine proteases, such as chymotrypsin. Thus, pH-dependence of, and kinetic deuterium isotope effects on, the rate constants indicated that the enzyme has two forms, which exhibit different activities and interconvert with changing pH. It can be concluded that a general base/acid-catalyzed acylation step is rate-limiting in the lower pH range, and an isotopically stlent step, probably a conformational change preceding the acylation dominates the reaction in the physiological PH range.

AB - Prolyl endopeptidase, an enzyme exhibiting high specificity towards the Pro-Xaa bond, is thought to play an important role in the metabolism of biologically active peptides. We have purified the enzyme from pig muscle and observed significant differences in its kinetic behavior as compared to the extensively studied serine proteases, such as chymotrypsin. Thus, pH-dependence of, and kinetic deuterium isotope effects on, the rate constants indicated that the enzyme has two forms, which exhibit different activities and interconvert with changing pH. It can be concluded that a general base/acid-catalyzed acylation step is rate-limiting in the lower pH range, and an isotopically stlent step, probably a conformational change preceding the acylation dominates the reaction in the physiological PH range.

UR - http://www.scopus.com/inward/record.url?scp=0025939693&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025939693&partnerID=8YFLogxK

M3 - Article

VL - 50

SP - 721

EP - 726

JO - Biomedica Biochimica Acta

JF - Biomedica Biochimica Acta

SN - 0232-766X

IS - 4-6

ER -