Literature summary for 1.1.1.27 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.

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Cloned(Commentary)

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

Inhibitors

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

Localization

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

Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum	-	-	-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Synonyms

Synonyms	Comment	Organism
lactate dehydrogenase	-	Plasmodium falciparum
LDH	-	Plasmodium falciparum

Expression

Organism	Comment	Expression
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

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Release 2023.1 (January 2023)