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Literature summary for 1.1.1.27 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

Protein Variants Comment Organism
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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and enlarged loop mutants ELM1 and ELM2 Plasmodium falciparum

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Cofactor

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