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Literature summary extracted from

  • Auerbach, G.; Ostendorp, R.; Prade, L.; Korndorfer, I.; Dams, T.; Huber, R.; Jaenicke, R.
    Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization (1998), Structure, 15, 769-781.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.27 2.1 A resolution as a quarternary complex with the cofactor NADH, the allosteric activator fructose-1,6-bisphosphate and the substrate analog oxamate Thermotoga maritima

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.27 pyruvate + NADH + H+ Thermotoga maritima last step in anaerobic glycolysis L-lactate + NAD+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Thermotoga maritima
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 pyruvate + NADH + H+
-
 Thermotoga maritima (S)-lactate + NAD+
-
 ?
1.1.1.27 pyruvate + NADH + H+ last step in anaerobic glycolysis Thermotoga maritima L-lactate + NAD+
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NADH coenzyme Thermotoga maritima