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.
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.
Zülli
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F
Inst. für Molekularbiologie und Biophysik, Eidg. Technische Hochschule, Zürich.
Weber
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H
Zuber
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H
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D001483:Base Sequence; D003001:Cloning, Molecular; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D007770:L-Lactate Dehydrogenase / Q000235:genetics*; D008969:Molecular Sequence Data; D013045:Species Specificity
D007770:L-Lactate Dehydrogenase