Steady‐state approximation of enzyme activation and inhibition

Masahiro Okamoto, Youko Takeda, Yoichi Aso, Katsuya Hayashi

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

This article deals with the effects of the initial concentration of effector (inhibitor or activator) on the steady‐state approximation of enzyme kinetics. The results could be summarized as follows: (1) In competitive inhibition, the increase in the initial concentration of inhibitor led to the reduction of steady state time. (2) In noncompetitive and uncompetitive inhibitions, the steady state time was not changed with the increase in the initial concentration of inhibitor. (3) In nonessential activation, the increase in the initial concentration of activator led to the reduction of steadystate time. (4) It was specially noted that in nonessential activation, even if the reaction is in the steady‐state, activation constant (KA) can not be determined exactly unless the initial concentration of activator is very small.

Original languageEnglish
Pages (from-to)1453-1463
Number of pages11
JournalBiotechnology and Bioengineering
Volume25
Issue number6
DOIs
Publication statusPublished - Jan 1 1983

Fingerprint

Enzyme inhibition
Enzyme Activation
Enzymes
Chemical activation
Enzyme kinetics

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this

Steady‐state approximation of enzyme activation and inhibition. / Okamoto, Masahiro; Takeda, Youko; Aso, Yoichi; Hayashi, Katsuya.

In: Biotechnology and Bioengineering, Vol. 25, No. 6, 01.01.1983, p. 1453-1463.

Research output: Contribution to journalArticle

Okamoto, Masahiro ; Takeda, Youko ; Aso, Yoichi ; Hayashi, Katsuya. / Steady‐state approximation of enzyme activation and inhibition. In: Biotechnology and Bioengineering. 1983 ; Vol. 25, No. 6. pp. 1453-1463.
@article{86d97f52b8b04aa6acc4fad4b05d74c2,
title = "Steady‐state approximation of enzyme activation and inhibition",
abstract = "This article deals with the effects of the initial concentration of effector (inhibitor or activator) on the steady‐state approximation of enzyme kinetics. The results could be summarized as follows: (1) In competitive inhibition, the increase in the initial concentration of inhibitor led to the reduction of steady state time. (2) In noncompetitive and uncompetitive inhibitions, the steady state time was not changed with the increase in the initial concentration of inhibitor. (3) In nonessential activation, the increase in the initial concentration of activator led to the reduction of steadystate time. (4) It was specially noted that in nonessential activation, even if the reaction is in the steady‐state, activation constant (KA) can not be determined exactly unless the initial concentration of activator is very small.",
author = "Masahiro Okamoto and Youko Takeda and Yoichi Aso and Katsuya Hayashi",
year = "1983",
month = "1",
day = "1",
doi = "10.1002/bit.260250604",
language = "English",
volume = "25",
pages = "1453--1463",
journal = "Biotechnology and Bioengineering",
issn = "0006-3592",
publisher = "Wiley-VCH Verlag",
number = "6",

}

TY - JOUR

T1 - Steady‐state approximation of enzyme activation and inhibition

AU - Okamoto, Masahiro

AU - Takeda, Youko

AU - Aso, Yoichi

AU - Hayashi, Katsuya

PY - 1983/1/1

Y1 - 1983/1/1

N2 - This article deals with the effects of the initial concentration of effector (inhibitor or activator) on the steady‐state approximation of enzyme kinetics. The results could be summarized as follows: (1) In competitive inhibition, the increase in the initial concentration of inhibitor led to the reduction of steady state time. (2) In noncompetitive and uncompetitive inhibitions, the steady state time was not changed with the increase in the initial concentration of inhibitor. (3) In nonessential activation, the increase in the initial concentration of activator led to the reduction of steadystate time. (4) It was specially noted that in nonessential activation, even if the reaction is in the steady‐state, activation constant (KA) can not be determined exactly unless the initial concentration of activator is very small.

AB - This article deals with the effects of the initial concentration of effector (inhibitor or activator) on the steady‐state approximation of enzyme kinetics. The results could be summarized as follows: (1) In competitive inhibition, the increase in the initial concentration of inhibitor led to the reduction of steady state time. (2) In noncompetitive and uncompetitive inhibitions, the steady state time was not changed with the increase in the initial concentration of inhibitor. (3) In nonessential activation, the increase in the initial concentration of activator led to the reduction of steadystate time. (4) It was specially noted that in nonessential activation, even if the reaction is in the steady‐state, activation constant (KA) can not be determined exactly unless the initial concentration of activator is very small.

UR - http://www.scopus.com/inward/record.url?scp=0020764555&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020764555&partnerID=8YFLogxK

U2 - 10.1002/bit.260250604

DO - 10.1002/bit.260250604

M3 - Article

AN - SCOPUS:0020764555

VL - 25

SP - 1453

EP - 1463

JO - Biotechnology and Bioengineering

JF - Biotechnology and Bioengineering

SN - 0006-3592

IS - 6

ER -