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Literature summary extracted from

  • Berwal, R.; Gopalan, N.; Chandel, K.; Prasad, G.B.; Prakash, S.
    Plasmodium falciparum: enhanced soluble expression, purification and biochemical characterization of lactate dehydrogenase (2008), Exp. Parasitol., 120, 135-141.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.27 into pQE-30 Xa vector and expressed in Escherichia coli SG13009 cells Plasmodium falciparum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.27 3-acetylpyridine adenine dinucleotide the enzyme exhibits characteristic reduced substrate inhibition and enhanced kcat Plasmodium falciparum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.27 additional information the recombinant protein is exclusively associated with inclusion bodies Plasmodium falciparum
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Plasmodium falciparum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.27 to homogeneity yielding 18 mg of protein/litre culture Plasmodium falciparum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.27 453.8
-
-
 Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
1.1.1.27 lactate dehydrogenase
-
 Plasmodium falciparum
1.1.1.27 LDH
-
 Plasmodium falciparum

Expression

EC Number Organism Comment Expression
1.1.1.27 Plasmodium falciparum the enzyme is induced at 37°C by 0.5 mM beta-D-thiogalactoside concentration being associated with inclusion bodies. By reducing cell growth temperature to 15°C and sopropyl beta-D-thiogalactoside concentration to 0.25 mM, it is possible to get approximately 82% of expressed protein in soluble form up