Reference on EC 1.1.1.27 - L-lactate dehydrogenase and Organism(s) Bifidobacterium longum and UniProt Accession P0CW93
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Iwata, S.; Yoshida, S.; Ohta, T.
A regular 1:1 complex of two allosteric states in the single crystal of L-lactate dehydrogenase from Bifidobacterium longum
J. Mol. Biol.
236
958-959
1994
Bifidobacterium longum
Iwata, S.; Kamata, K.; Yoshida, S.; Minowa, T.; Ohta, T.
T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control
Nat. Struct. Biol.
1
176-185
1994
Bifidobacterium longum
Ishida, N.; Saitoh, S.; Tokuhiro, K.; Nagamori, E.; Matsuyama, T.; Kitamoto, K.; Takahashi, H.
Efficient production of L-Lactic acid by metabolically engineered Saccharomyces cerevisiae with a genome-integrated L-lactate dehydrogenase gene
Appl. Environ. Microbiol.
71
1964-1970
2005
Bos taurus, Bifidobacterium longum (P0CW93), Bifidobacterium longum