Cloning, sequencing and comparison of three lactococcal L-lactate dehydrogenase genes.

@article{Swindell1994CloningSA,
  title={Cloning, sequencing and comparison of three lactococcal L-lactate dehydrogenase genes.},
  author={Simon R. Swindell and Hugh G. Griffin and Michael John Gasson},
  journal={Microbiology},
  year={1994},
  volume={140 ( Pt 6)},
  pages={
          1301-5
        }
}
The conversion of pyruvate to lactate is a key feature of lactococcal strains. The enzyme which facilitates this conversion, L-lactate dehydrogenase (LDH), and the gene which encodes it (Idh), are therefore of great significance. This paper presents the cloning and DNA sequence analysis of three further lactococcal genes which are of key importance in the genetic manipulation of commercial starter strains. The Idh gene from Lactococcus lactis subsp. Lactis biovar diacetylactis BU2-60 has been… 
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TLDR
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This study has expressed from a plasmid the ilvBN genes, which encode the other α-acetolactate synthase (IlvBN), and IlvBN, with a Km value of 8.3 mM, was shown to have a greater affinity for pyruvate than does Als.
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A gene located downstream of the dnaK operon in strain MG1363, named orf4, was shown not to be regulated by heat shock, and the induction kinetics observed for ftsH suggested a different regulation for this gene.
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References

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Cloning and sequence analysis of the gene encoding L-lactate dehydrogenase from Lactococcus lactis: evolutionary relationships between 21 different LDH enzymes.
Structure and function of L-lactate dehydrogenases from thermophilic, mesophilic and psychrophilic bacteria, IX. Identification, isolation and nucleotide sequence of two L-lactate dehydrogenase genes of the psychrophilic bacterium Bacillus psychrosaccharolyticus.
Two genes encoding for L-lactate dehydrogenase (LDH) from the psychrophilic bacterium Bacillus psychrosaccharolyticus (DSM 6) were cloned and their nucleotide sequence determined using a pEMBL vector…
Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site.
Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site.
Development and application of oligonucleotide probes for identification of Lactococcus lactis subsp. cremoris
TLDR
The purpose was to identify unique rRNA sequences that could be used to discriminate L. lactis subsp.
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. megat
TLDR
The lactate dehydrogenase (LDH) gene of a mesophilic bacterium, Bacillus megaterium, was cloned in E. coli HB 101 using a pEMBL vector and synthetic oligonucleotide probes and the gene and its 5' and 3' flanking regions have been sequenced.
Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus L-lactate dehydrogenase gene.
Cloning and expression of the gene encoding the fructose-1,6-diphosphate-dependent L-(+)-lactate dehydrogenase of Streptococcus mutans
TLDR
The ability to clone this gene is expected to have great practical significance in the construction of an effector strain for use in the replacement therapy of dental caries and could complement a mutation in the fermentative D-(-)-LDH of Escherichia coli.
Cloning and DNA sequence analysis of an X-prolyl dipeptidyl aminopeptidase gene from Lactococcus lactis subsp. lactis NCDO 763
TLDR
Comparison of the amino-terminal sequence of the X-PDAP enzyme with the amino acid sequence deduced from the pepXP gene indicated that the enzyme is not subjected to posttranslational modification or exported via processing of a signal peptide.
Amino acid sequence of the L-lactate dehydrogenase of Bacillus caldotenax deduced from the nucleotide sequence of the cloned gene.
TLDR
The deduced amino acid sequence of the L-lactate dehydrogenase (LDH) from B. caldotenax predicted a protein of 317 amino acid residues; comparison with the B. stearothermophilus enzyme revealed only 30 amino acid differences between the two enzymes; thus the enzymes are 90.4% homologous.
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