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Literature summary for 1.1.1.27 extracted from

  • Chen, N.H.; Ong, C.Y.; Osullivan, J.; Ibranovic, I.; Davey, K.; Edwards, J.L.; McEwan, A.G.
    Two distinct L-lactate dehydrogenases play a role in the survival of Neisseria gonorrhoeae in cervical epithelial cells (2020), J. Infect. Dis., 221, 449-453 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Neisseria gonorrhoeae Q5F885 and Q5F884 and Q5F883 Q5F885 i.e. oxidoreductase domain, Q5F884 i.e. LUD_dom domain-containing protein, Q5F883 i.e. (Fe-S)-binding protein
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Neisseria gonorrhoeae ATCC 700825 Q5F885 and Q5F884 and Q5F883 Q5F885 i.e. oxidoreductase domain, Q5F884 i.e. LUD_dom domain-containing protein, Q5F883 i.e. (Fe-S)-binding protein
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Synonyms

Synonyms Comment Organism
LutACB
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Neisseria gonorrhoeae
NGO0904
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Neisseria gonorrhoeae
NGO0905
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Neisseria gonorrhoeae
NGO0906
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Neisseria gonorrhoeae

Cofactor

Cofactor Comment Organism Structure
Fe-S center
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Neisseria gonorrhoeae

Expression

Organism Comment Expression
Neisseria gonorrhoeae expression of LutACB is induced by iron-limited conditions up

General Information

General Information Comment Organism
physiological function the growth of the LutACB mutants is similar to that of the wild-type strain on L-lactate. The isoforms LutACB/LldD double mutant fails to grow on L-lactate, and complementation of this strain with LutACB restores growth to wild-type levels. LutACB contributes to L-lactate dehydrogenase activity under iron-replete conditions, and the LutACB deletion mutant is impaired in its ability to survive within human primary cervical epithelial cells Neisseria gonorrhoeae