Plasmodium berghei L-lactate dehydrogenase

What is Plasmodium berghei L-lactate dehydrogenase and its biological function

Plasmodium berghei L-lactate dehydrogenase (PLDH) is an enzyme that is expressed in the parasites that cause malaria, specifically Plasmodium berghei. It is a member of the lactate dehydrogenase (LDH) family of enzymes, which play a role in the metabolism of lactate. PLDH is composed of a catalytic domain that is responsible for its enzymatic activity and a non-catalytic domain that is involved in its function.

PLDH plays a critical role in the metabolism of lactate by catalyzing the conversion of pyruvate to lactate. This process is known as the Cori cycle, which plays a role in the production of energy in the parasite. PLDH has been found to be essential for the survival and growth of the parasite, and therefore represents a potential target for the development of anti-malarial drugs.

There have been a number of recent research studies focused on PLDH and its role in the development of malaria. For example, a study published in the journal Nature Communications in 2021 found that targeting PLDH with small molecule inhibitors was effective in reducing the growth and proliferation of P. berghei parasites in preclinical models.

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  • Product Name
  • Organism
  • Tag (Tag info)
  • Expression Host (Source)
  1. Recombinant Plasmodium berghei L-lactate dehydrogenase(PB000185.00.0)
    Plasmodium berghei (strain Anka)
    N-terminal 10xHis-tagged and C-terminal Myc-tagged
    E.coli

    Recombinant Plasmodium berghei L-lactate dehydrogenase(PB000185.00.0)

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