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Literature summary extracted from

  • Hewitt, C.O.; Sessions, R.B.; Dafforn, T.R.; Holbrook, J.J.
    Protein engineering tests of a homology model of Plasmodium falciparum lactate dehydrogenase (1997), Protein Eng., 10, 39-44.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.27 S163L decrease in substrate inhibition, the Km value for pyruvate is increased substantially and the turnover number is 60% that of wild type Plasmodium falciparum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.27 additional information lack of substrate inhibition Plasmodium falciparum
1.1.1.27 pyruvate substrate inhibition in wild type enzyme, lower substrate inhibition in mutant S163L Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.27 additional information
-
 additional information KM-values for mutant enzymes with enlarged loop Plasmodium falciparum
1.1.1.27 0.018
-
 NADH wild-type enzyme Plasmodium falciparum
1.1.1.27 0.065
-
 NADH mutant enzyme S163L 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 wild-type and enlarged loop mutants ELM1 and ELM2 Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 4-methyl-2-oxopentanoate + NADH
-
 Plasmodium falciparum 2-hydroxy-4-methylpentanoate + NAD+
-
 ?
1.1.1.27 phenylpyruvate + NADH
-
 Plasmodium falciparum 2-hydroxy-3-phenylpropanoate + NAD+
-
 ?
1.1.1.27 pyruvate + NADH + H+
-
 Plasmodium falciparum (S)-lactate + NAD+
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.27 additional information
-
 additional information turnover-numbers for mutant enzymes with enlarged loop Plasmodium falciparum
1.1.1.27 0.33
-
 4-methyl-2-oxopentanoate wild-type enzyme Plasmodium falciparum
1.1.1.27 39.5
-
 phenylpyruvate wild-type enzyme Plasmodium falciparum
1.1.1.27 180
-
 pyruvate wild-type enzyme Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 3-acetylpyridine adenine dinucleotide wild-type and S163 L mutant protein bind 3-acetylpyridine adenine dinucleotide more tightly than they bind NADH Plasmodium falciparum
1.1.1.27 NADH coenzyme Plasmodium falciparum