Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.27 extracted from

  • Ferrer, S.; Silla, E.; Tunon, I.; Oliva, M.; Moliner, V.; Williams, I.H.
    Dependence of enzyme reaction mechanism on protonation state of titratable residues and QM level description: lactate dehydrogenase (2005), Chem. Commun. (Camb.), 2005, 5873-5875.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + NADH + H+ study of the dependence of the chemical reaction mechanism of lactate dehydrogenase on the protonation state of titratable residues and on the level of the quantum mechanical description by means of hybrid quantum-mechanical methods Geobacillus stearothermophilus (S)-lactate + NAD+
-
?

Cofactor

Cofactor Comment Organism Structure
NADH
-
Geobacillus stearothermophilus