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Literature summary for 1.1.1.27 extracted from

  • Kavanagh, K.L.; Elling, R.A.; Wilson, D.K.
    Structure of Toxoplasma gondii LDH1: active-site differences from human lactate dehydrogenases and the structural basis for efficient APAD+ use (2004), Biochemistry, 43, 879-889.
    View publication on PubMed

Application

Application Comment Organism
medicine structural characterization of the enzyme and active-site differences from the human lactate dehydrogenase may be useful for structural-based design of new treatments for toxoplasmic infections Toxoplasma gondii

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Toxoplasma gondii

Crystallization (Commentary)

Crystallization (Comment) Organism
in apo-form and in ternary complexes containing NAD+ or NAD+-analogue 3-acetylpyridine adenine dinucleotide and sulfate or the inhibitor oxalate Toxoplasma gondii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate + NADH + H+ Toxoplasma gondii terminal enzyme in aerobic glycolysis necessary for NAD+ regeneration (S)-lactate + NAD+
-
?

Organism

Organism UniProt Comment Textmining
Toxoplasma gondii P90613
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Toxoplasma gondii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + NADH + H+
-
Toxoplasma gondii (S)-lactate + NAD+
-
?
pyruvate + NADH + H+ terminal enzyme in aerobic glycolysis necessary for NAD+ regeneration Toxoplasma gondii (S)-lactate + NAD+
-
?

Synonyms

Synonyms Comment Organism
LDH1
-
Toxoplasma gondii

Cofactor

Cofactor Comment Organism Structure
NADH
-
Toxoplasma gondii