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

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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.

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References

  • Barstow DA, Clarke, AR, Chia WN (1986) Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus. Gene 46: 47-55.

    Google Scholar 

  • Clarke AR, Evington JRN, Dunn CR, Atkinson T, Holbrook JJ (1986) The molecular pathway by which fructose 1,6 bisphosphate induces the assembly of bacterial lactate dehydrogenase. Biochim. Biophys. Acta 870: 112-126.

    Google Scholar 

  • Clarke AR, Waldman ADB, Munro I, Holbrook JJ (1985) Changes in the state of subunit association of lactate dehydrogenase from Bacillus stearothermophilus. Biochim. Biophys. Acta 828: 375-379.

    Google Scholar 

  • Cleland WW (1970) Enzyme kinetics. In: Boyer PD, ed. The Enzymes, Vol. 3. New York: Academic Press, pp. 1-200.

    Google Scholar 

  • Duncan MJ, Hillman JD (1994). DNA sequence and inactivation of the gene encoding the fructose diphosphate dependent L-lactate dehydrogenase of Streptococcus mutans. Genembl Accession No. M72545.

  • Eszes CM, Sessions RB, Clarke AR, Moreton KM, Holbrook JJ (1996) Removal of substrate inhibition in a lactate dehydrogenase from human muscle by a single residue change. FEBS Lett. 399: 193-197.

    Google Scholar 

  • Hewitt CO, Eszes CM, Sessions RB, Moreton KM, Dafforn TR, Takei J, Dempsey CE, Clarke AR, Holbrook JJ (1999) A general method for relieving substrate inhibition in lactate dehydrogenases. Prot. Eng. 12: 491-496.

    Google Scholar 

  • Hewitt CO, Sessions RB, Dafforn TR, Holbrook JJ (1997) Protein engineering tests of a homology model of Plasmodium falciparum lactate dehydrogenase. Prot. Eng. 10: 39-41.

    Google Scholar 

  • Holbrook JJ, Liljas A, Steindel S, Rossman MG (1975). Lactate dehydrogenase. In: Boyer PD, ed. The Enzymes, Vol. 11. New York: Academic Press, pp. 191-292.

    Google Scholar 

  • Leatherbarrow RJ (1987) Elsevier-BIOSOFT, ENZFITTER. A Nonlinear Regression Data Analysis Program for the IBM-PC. UK: Cambridge.

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Author notes

  1. Nevin Gül-Karagüler

    Present address: Fen-Edebiyat Fakultesi, Moleküler Biyoloji ve Genetik Bölümü, Istanbul Teknik Universitesi, Istanbul, Turkey

Authors and Affiliations

  1. Department of Biochemistry, School of Medical Sciences, University Walk, Bristol, BS8 1TD, UK

    Richard B. Sessions & J. John Holbrook

Authors
  1. Nevin Gül-Karagüler
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  2. Richard B. Sessions
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  3. J. John Holbrook
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Gül-Karagüler, N., Sessions, R.B. & Holbrook, J.J. Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus. Biotechnology Letters 23, 395–399 (2001). https://doi.org/10.1023/A:1005687723905

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  • DOI: https://doi.org/10.1023/A:1005687723905

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