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Literature summary for 1.1.1.27 extracted from

  • Deng, H.; Brewer, S.; Vu, D.M.; Clinch, K.; Callender, R.; Dyer, R.B.
    On the pathway of forming enzymatically productive ligand-protein complexes in lactate dehydrogenase (2008), Biophys. J., 95, 804-813.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Sus scrofa
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-
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Source Tissue

Source Tissue Comment Organism Textmining
heart
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Sus scrofa
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxamate + NADH two distinct active site LDH/NADH-oxamate complex conformations, a major populated structure wherein all significant hydrogen-bonding patterns are formed at the active site between protein and bound ligand necessary for the catalytically productive Michaelis complex and, a minor structure in a configuration of the active site that is unfavorable to carry out catalyzed chemistry. This latter structure likely simulates a dead-end complex in the reaction mixture. The evolution of the encounter complex between LDH/NADH and oxamate collapses via a branched reaction pathway to form the major and minor bound species. Once the encounter complex is formed between LDH/NADH and substrate, the ternary protein-ligand complex appears to fold to form a compact productive complex in an all or nothing like fashion with all the important molecular interactions coming together at the same time Sus scrofa ?
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?

Synonyms

Synonyms Comment Organism
lactate dehydrogenase
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Sus scrofa
LDH
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Sus scrofa

Cofactor

Cofactor Comment Organism Structure
NADH
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Sus scrofa