Biol Chem Hoppe Seyler. 1987 Sep;368(9):1167-77.

Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, VI. Nucleotide sequences of lactate dehydrogenase genes from the thermophilic bacteria Bacillus stearothermophilus, B. caldolyticus and B. caldotenax.

Inst. für Molekularbiologie und Biophysik, Eidg. Technische Hochschule, Zürich.

Based on the previously determined amino-acid sequence of lactate dehydrogenase from B. stearothermophilus, an oligonucleotide probe was synthesized and used to clone the structural genes for lactate dehydrogenase from B. stearothermophilus, B. caldolyticus and B. caldotenax. The nucleotide sequences of the entire LDH genes from these three thermophilic bacilli were determined by the method of Maxam and Gilbert. The nucleotide sequence of the LDH gene from B. stearothermophilus is exactly identical to the one published recently; it agrees with the experimentally determined amino-acid sequence except at three positions. The amino-acid homologies among these thermophilic enzymes are 90% or more. The LDH genes are efficiently expressed in E. coli.

PMID: 3675869 [PubMed - indexed for MEDLINE]

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Amino acid sequence of the L-lactate dehydrogenase of Bacillus caldotenax deduced from the nucleotide sequence of the cloned gene.
Eur J Biochem. 1987 Jun 15; 165(3):581-6.

[Eur J Biochem. 1987]
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. VII. Nucleotide sequence of the lactate dehydrogenase gene from the mesophilic bacterium Bacillus megaterium. Preparation and properties of a hybrid lactate dehydrogenase comprising moieties of the B. megaterium and B. stearothermophilus enzymes.
Biol Chem Hoppe Seyler. 1987 Oct; 368(10):1391-9.

[Biol Chem Hoppe Seyler. 1987]
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, X. Analysis of structural elements responsible for the differences in thermostability and activation by fructose 1,6-bisphosphate in the lactate dehydrogenases from B. stearothermophilus and B. caldolyticus by protein engineering.
Biol Chem Hoppe Seyler. 1990 Aug; 371(8):655-62.

[Biol Chem Hoppe Seyler. 1990]
ReviewTemperature adaptation of lactate dehydrogenase. Structural, functional and genetic aspects.
Biophys Chem. 1988 Feb; 29(1-2):171-9.

[Biophys Chem. 1988]
ReviewThe structural domains in the E2 component of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus.
Biochem Soc Trans. 1991 Nov; 19(4):917-22.

[Biochem Soc Trans. 1991]
» See reviews... | » See all...

Cited by 3 PubMed Central articles

Malate dehydrogenase from the mesophile Chlorobium vibrioforme and from the mild thermophile Chlorobium tepidum: molecular cloning, construction of a hybrid, and expression in Escherichia coli.
Naterstad K, Lauvrak V, Sirevåg R. J Bacteriol. 1996 Dec; 178(24):7047-52.

[J Bacteriol. 1996]
Evolutionary implications of the cDNA sequence of the single lactate dehydrogenase of a lamprey.
Stock DW, Whitt GS. Proc Natl Acad Sci U S A. 1992 Mar 1; 89(5):1799-803.

[Proc Natl Acad Sci U S A. 1992]
Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread.
Vazquez-Boland JA, Kocks C, Dramsi S, Ohayon H, Geoffroy C, Mengaud J, Cossart P. Infect Immun. 1992 Jan; 60(1):219-30.

[Infect Immun. 1992]

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Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, VI. Nucleotide sequences of lactate dehydrogenase genes from the thermophilic bacteria Bacillus stearothermophilus, B. caldolyticus and B. caldotenax.

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