Role of reduced glutathione in the Δ5-3-ketosteroid isomerase reaction of liver

Ann M. Benson, Paul Talalay

Research output: Contribution to journalArticle

Abstract

Partially purified rat liver Δ5-3-ketosteroid isomerase (EC 5.3.3.1) is profoundly and specifically activated by reduced glutathione (GSH). This stimulating effect shows normal saturating kinetics, and both Km and Vmax are pH-dependent. The binding of GSH is independent of the concentration of Δ5-androstene-3,17-dione, whereas the Km for Δ5-androstene-3,17-dione is markedly reduced by saturating levels of GSH. The same catalytic site appears to isomerize both Δ5-androstene-3,17-dione and Δ5-pregnene-3,20-dione. Several steroidal inhibitors compete with Δ5-androstene-3,17-dione, whereas S-methyl-glutathione competes with GSH. This activation of Δ5-3-ketosteroid isomerase is also observed in the livers of other species (calf, guinea pig, human), and represents a hitherto unrecognized function of reduced glutathione.

Original languageEnglish (US)
Pages (from-to)1073-1079
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume69
Issue number4
DOIs
StatePublished - Apr 19 1976

Fingerprint

steroid delta-isomerase
Liver
Glutathione
Pregnenes
Rats
Catalytic Domain
Guinea Pigs
Chemical activation
Kinetics
5-androstene-3,17-dione

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Role of reduced glutathione in the Δ5-3-ketosteroid isomerase reaction of liver. / Benson, Ann M.; Talalay, Paul.

In: Biochemical and Biophysical Research Communications, Vol. 69, No. 4, 19.04.1976, p. 1073-1079.

Research output: Contribution to journalArticle

@article{a4a964ec64d34715bb88f5c10d637006,
title = "Role of reduced glutathione in the Δ5-3-ketosteroid isomerase reaction of liver",
abstract = "Partially purified rat liver Δ5-3-ketosteroid isomerase (EC 5.3.3.1) is profoundly and specifically activated by reduced glutathione (GSH). This stimulating effect shows normal saturating kinetics, and both Km and Vmax are pH-dependent. The binding of GSH is independent of the concentration of Δ5-androstene-3,17-dione, whereas the Km for Δ5-androstene-3,17-dione is markedly reduced by saturating levels of GSH. The same catalytic site appears to isomerize both Δ5-androstene-3,17-dione and Δ5-pregnene-3,20-dione. Several steroidal inhibitors compete with Δ5-androstene-3,17-dione, whereas S-methyl-glutathione competes with GSH. This activation of Δ5-3-ketosteroid isomerase is also observed in the livers of other species (calf, guinea pig, human), and represents a hitherto unrecognized function of reduced glutathione.",
author = "Benson, {Ann M.} and Paul Talalay",
year = "1976",
month = "4",
day = "19",
doi = "10.1016/0006-291X(76)90482-4",
language = "English (US)",
volume = "69",
pages = "1073--1079",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "4",

}

TY - JOUR

T1 - Role of reduced glutathione in the Δ5-3-ketosteroid isomerase reaction of liver

AU - Benson, Ann M.

AU - Talalay, Paul

PY - 1976/4/19

Y1 - 1976/4/19

N2 - Partially purified rat liver Δ5-3-ketosteroid isomerase (EC 5.3.3.1) is profoundly and specifically activated by reduced glutathione (GSH). This stimulating effect shows normal saturating kinetics, and both Km and Vmax are pH-dependent. The binding of GSH is independent of the concentration of Δ5-androstene-3,17-dione, whereas the Km for Δ5-androstene-3,17-dione is markedly reduced by saturating levels of GSH. The same catalytic site appears to isomerize both Δ5-androstene-3,17-dione and Δ5-pregnene-3,20-dione. Several steroidal inhibitors compete with Δ5-androstene-3,17-dione, whereas S-methyl-glutathione competes with GSH. This activation of Δ5-3-ketosteroid isomerase is also observed in the livers of other species (calf, guinea pig, human), and represents a hitherto unrecognized function of reduced glutathione.

AB - Partially purified rat liver Δ5-3-ketosteroid isomerase (EC 5.3.3.1) is profoundly and specifically activated by reduced glutathione (GSH). This stimulating effect shows normal saturating kinetics, and both Km and Vmax are pH-dependent. The binding of GSH is independent of the concentration of Δ5-androstene-3,17-dione, whereas the Km for Δ5-androstene-3,17-dione is markedly reduced by saturating levels of GSH. The same catalytic site appears to isomerize both Δ5-androstene-3,17-dione and Δ5-pregnene-3,20-dione. Several steroidal inhibitors compete with Δ5-androstene-3,17-dione, whereas S-methyl-glutathione competes with GSH. This activation of Δ5-3-ketosteroid isomerase is also observed in the livers of other species (calf, guinea pig, human), and represents a hitherto unrecognized function of reduced glutathione.

UR - http://www.scopus.com/inward/record.url?scp=0017062681&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017062681&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(76)90482-4

DO - 10.1016/0006-291X(76)90482-4

M3 - Article

C2 - 6023

AN - SCOPUS:0017062681

VL - 69

SP - 1073

EP - 1079

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -