Literature summary for 1.1.1.27 extracted from

Svedruzic, Z.M.; Odorcic, I.; Chang, C.H.; Svedruzic, D.
Substrate channeling via a transient protein-protein complex The case of D-glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase (2020), Sci. Rep., 10, 10404 .

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Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	P13491	-	-

General Information

General Information	Comment	Organism
metabolism	LDH activity with free NADH and GAPDH-NADH complex always take place in parallel. NADH-channeling from D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to L-lactate dehydrogenase (LDH) is observed only in assays that mimic cytosolic conditions where free NADH concentration is negligible and the GAPDH-NADH complex is dominant. LDH and GAPDH can form a leaky channeling complex only at the limiting NADH concentrations. A positive electric field between the NAD(H) binding sites on LDH and GAPDH tetramers can merge in the LDH-GAPDH complex	Oryctolagus cuniculus

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Release 2023.1 (January 2023)