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Literature summary for 1.1.1.27 extracted from

  • Pineda, J.R.; Callender, R.; Schwartz, S.D.
    Ligand binding and protein dynamics in lactate dehydrogenase (2007), Biophys. J., 93, 1474-1483.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
binary complex of LDH with the cofactor NADH and the LDH/NADH-oxamate ternary complex, molecular dynamics, and simulation model from crystal structure at 2.1 A resolution, Protein DataBank entry 1IOZ, overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lactate + NAD+ Homo sapiens
-
pyruvate + NADH
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lactate + NAD+
-
Homo sapiens pyruvate + NADH
-
r
L-lactate + NAD+ LDH binds its substrate via the formation of a LDH/NADH-substrate encounter complex through a select-fit mechanism, whereby only a minority population of LDH/NADH is binding-competent, molecular dynamics calculations to explore the variations in structure accessible to the binary complex and binding-competent structures, active site interactions in the ternary complex, overview Homo sapiens pyruvate + NADH
-
r

Subunits

Subunits Comment Organism
More binary complex of LDH with the cofactor NADH and the LDH/NADH-oxamate ternary complex, molecular dynamics, and simulation model from crystal structure at 2.1 A resolution, Protein DataBank entry 1IOZ, overview Homo sapiens

Synonyms

Synonyms Comment Organism
lactate dehydrogenase
-
Homo sapiens
LDH
-
Homo sapiens