Cloning and nucleotide sequencing of L-lactate dehydrogenase gene from Streptococcus thermophilus M-192.
The gene encoding L-lactate dehydrogenase (LDH) was cloned from an industrial dairy strain of Streptococcus thermophilus M-192 using a synthetic oligonucleotide probe based on the N-terminal amino acid sequence of the purified enzyme, and its nucleotide sequence was determined. The enzyme was deduced to have 328 amino acid residues with a molecular weight of 35,428 and found to have high sequence similarity to LDHs from other lactic acid bacteria (89.0% to Streptococcus mutans, 76.3% to Lactococcus lactis subsp. lactis, 67% to Lactobacillus casei, and 60% to Lactobacillus plantarum). The gene contained a promoter-like sequence similar to the Escherichia coli promoter consensus, and expression of the S. thermophilus LDH gene was observed in E. coli cells.
Ito
Y
Y
Meiji Institute of Health Science, Meiji Milk Products Co., Ltd., Odawara, Japan.
Sasaki
T
T
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D003062:Codon; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D015870:Gene Expression; D007770:L-Lactate Dehydrogenase / Q000235:genetics*; D007778:Lactobacillus / Q000201:enzymology / Q000235:genetics; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013291:Streptococcus / Q000201:enzymology* / Q000235:genetics*; D013295:Streptococcus mutans / Q000201:enzymology / Q000235:genetics
D001426:Bacterial Proteins; D003062:Codon; D007770:L-Lactate Dehydrogenase