Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus

Nevin Gül-Karagüler; Richard B. Sessions; J. John Holbrook

doi:10.1023/A:1005687723905

Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus

Nevin Gül-Karagüler^*
, Richard B. Sessions
, J. John Holbrook

^*Corresponding author for this work

Department of Molecular Biology and Genetics

University Walk

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

A single residue of the NAD(H)-dependent lactate dehydrogenase (LDH) from Bacillus stearothermophilus has been changed in order to decrease substrate inhibition. The conserved aspartic acid residue at position 52 was replaced by glutamate using site-directed mutagenesis. The effect on substrate inhibition was measured. In the glutamate-52 mutant substrate inhibition is decreased twofold.

Original language	English
Pages (from-to)	395-399
Number of pages	5
Journal	Biotechnology Letters
Volume	23
Issue number	5
DOIs	https://doi.org/10.1023/A:1005687723905
Publication status	Published - 2001

Keywords

Lactate dehydrogenase
Site-directed mutagenesis
Substrate inhibition

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10.1023/A:1005687723905

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title = "Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus",

abstract = "A single residue of the NAD(H)-dependent lactate dehydrogenase (LDH) from Bacillus stearothermophilus has been changed in order to decrease substrate inhibition. The conserved aspartic acid residue at position 52 was replaced by glutamate using site-directed mutagenesis. The effect on substrate inhibition was measured. In the glutamate-52 mutant substrate inhibition is decreased twofold.",

keywords = "Lactate dehydrogenase, Site-directed mutagenesis, Substrate inhibition",

author = "Nevin G{\"u}l-Karag{\"u}ler and Sessions, \{Richard B.\} and Holbrook, \{J. John\}",

year = "2001",

doi = "10.1023/A:1005687723905",

language = "English",

volume = "23",

pages = "395--399",

journal = "Biotechnology Letters",

issn = "0141-5492",

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T1 - Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus

AU - Gül-Karagüler, Nevin

AU - Sessions, Richard B.

AU - Holbrook, J. John

PY - 2001

Y1 - 2001

N2 - A single residue of the NAD(H)-dependent lactate dehydrogenase (LDH) from Bacillus stearothermophilus has been changed in order to decrease substrate inhibition. The conserved aspartic acid residue at position 52 was replaced by glutamate using site-directed mutagenesis. The effect on substrate inhibition was measured. In the glutamate-52 mutant substrate inhibition is decreased twofold.

AB - A single residue of the NAD(H)-dependent lactate dehydrogenase (LDH) from Bacillus stearothermophilus has been changed in order to decrease substrate inhibition. The conserved aspartic acid residue at position 52 was replaced by glutamate using site-directed mutagenesis. The effect on substrate inhibition was measured. In the glutamate-52 mutant substrate inhibition is decreased twofold.

KW - Lactate dehydrogenase

KW - Site-directed mutagenesis

KW - Substrate inhibition

UR - https://www.scopus.com/pages/publications/0035120153

U2 - 10.1023/A:1005687723905

DO - 10.1023/A:1005687723905

M3 - Article

AN - SCOPUS:0035120153

SN - 0141-5492

VL - 23

SP - 395

EP - 399

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 5

ER -

Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus

Abstract

Keywords

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