Effect of pressure on catalytic properties of glutamate racemase from Aquifex pyrophilus, an extremophilic bacteria

A. Lee, Ki Seog, Young Min Chi, Yeon Gyu Yu

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The effect of pressure on the catalytic properties of glutamate racemase from Aquifex pyrophilus, an extremophilic bacterium, was investigated. The activation volume for the overall reaction (ΔV) and catalysis (ΔVcat) was -96.97 ml/mol and 4.97 ml/mol, respectively, while the reaction volume for the substrate binding (ΔVKm-1) was -101.94 ml/mol. The large negative ΔV for the overall reaction indicated that the pressurization of glutamate racemase resulted in enhanced catalytic efficiencies. In addition, this value was also due to the large negative ΔVKm-1 for the substrate binding. The negative value of ΔVKm-1 implied that the conformational changes in the enzyme molecule occurred during the substrate binding process, thereby increasing the degree of hydration. The small value of ΔVcat suggested that the pressure did not affect the glutamate racemase catalysis after the substrate binding.

Original languageEnglish
Pages (from-to)149-152
Number of pages4
JournalJournal of Microbiology and Biotechnology
Volume12
Issue number1
Publication statusPublished - 2002 Jan 1

Fingerprint

glutamate racemase
Catalysis
Bacteria
Pressure
Substrates
Pressurization
Hydration
Enzymes
Chemical activation
Molecules

Keywords

  • Activation volume
  • Aquifex pyrophilus
  • Extremophiles
  • Glutamate racemase
  • High pressure

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

Effect of pressure on catalytic properties of glutamate racemase from Aquifex pyrophilus, an extremophilic bacteria. / Lee, A.; Seog, Ki; Chi, Young Min; Yu, Yeon Gyu.

In: Journal of Microbiology and Biotechnology, Vol. 12, No. 1, 01.01.2002, p. 149-152.

Research output: Contribution to journalArticle

@article{74762b5e2cfe412bb1a93f89068c9c9b,
title = "Effect of pressure on catalytic properties of glutamate racemase from Aquifex pyrophilus, an extremophilic bacteria",
abstract = "The effect of pressure on the catalytic properties of glutamate racemase from Aquifex pyrophilus, an extremophilic bacterium, was investigated. The activation volume for the overall reaction (ΔV≠) and catalysis (ΔV≠cat) was -96.97 ml/mol and 4.97 ml/mol, respectively, while the reaction volume for the substrate binding (ΔVKm-1) was -101.94 ml/mol. The large negative ΔV≠ for the overall reaction indicated that the pressurization of glutamate racemase resulted in enhanced catalytic efficiencies. In addition, this value was also due to the large negative ΔVKm-1 for the substrate binding. The negative value of ΔVKm-1 implied that the conformational changes in the enzyme molecule occurred during the substrate binding process, thereby increasing the degree of hydration. The small value of ΔV≠cat suggested that the pressure did not affect the glutamate racemase catalysis after the substrate binding.",
keywords = "Activation volume, Aquifex pyrophilus, Extremophiles, Glutamate racemase, High pressure",
author = "A. Lee and Ki Seog and Chi, {Young Min} and Yu, {Yeon Gyu}",
year = "2002",
month = "1",
day = "1",
language = "English",
volume = "12",
pages = "149--152",
journal = "Journal of Microbiology and Biotechnology",
issn = "1017-7825",
publisher = "Korean Society for Microbiolog and Biotechnology",
number = "1",

}

TY - JOUR

T1 - Effect of pressure on catalytic properties of glutamate racemase from Aquifex pyrophilus, an extremophilic bacteria

AU - Lee, A.

AU - Seog, Ki

AU - Chi, Young Min

AU - Yu, Yeon Gyu

PY - 2002/1/1

Y1 - 2002/1/1

N2 - The effect of pressure on the catalytic properties of glutamate racemase from Aquifex pyrophilus, an extremophilic bacterium, was investigated. The activation volume for the overall reaction (ΔV≠) and catalysis (ΔV≠cat) was -96.97 ml/mol and 4.97 ml/mol, respectively, while the reaction volume for the substrate binding (ΔVKm-1) was -101.94 ml/mol. The large negative ΔV≠ for the overall reaction indicated that the pressurization of glutamate racemase resulted in enhanced catalytic efficiencies. In addition, this value was also due to the large negative ΔVKm-1 for the substrate binding. The negative value of ΔVKm-1 implied that the conformational changes in the enzyme molecule occurred during the substrate binding process, thereby increasing the degree of hydration. The small value of ΔV≠cat suggested that the pressure did not affect the glutamate racemase catalysis after the substrate binding.

AB - The effect of pressure on the catalytic properties of glutamate racemase from Aquifex pyrophilus, an extremophilic bacterium, was investigated. The activation volume for the overall reaction (ΔV≠) and catalysis (ΔV≠cat) was -96.97 ml/mol and 4.97 ml/mol, respectively, while the reaction volume for the substrate binding (ΔVKm-1) was -101.94 ml/mol. The large negative ΔV≠ for the overall reaction indicated that the pressurization of glutamate racemase resulted in enhanced catalytic efficiencies. In addition, this value was also due to the large negative ΔVKm-1 for the substrate binding. The negative value of ΔVKm-1 implied that the conformational changes in the enzyme molecule occurred during the substrate binding process, thereby increasing the degree of hydration. The small value of ΔV≠cat suggested that the pressure did not affect the glutamate racemase catalysis after the substrate binding.

KW - Activation volume

KW - Aquifex pyrophilus

KW - Extremophiles

KW - Glutamate racemase

KW - High pressure

UR - http://www.scopus.com/inward/record.url?scp=0036202409&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036202409&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0036202409

VL - 12

SP - 149

EP - 152

JO - Journal of Microbiology and Biotechnology

JF - Journal of Microbiology and Biotechnology

SN - 1017-7825

IS - 1

ER -