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Results 1 - 10 of 13 > >>
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EC Number Cofactor Commentary Reference
Show all pathways known for 1.1.1.375Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.375NAD(P)H the cofactor is bound at the active site 728123
Show all pathways known for 1.1.1.375Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.375NAD+ preference of NADP(H) over NAD(H). The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases 728123
Show all pathways known for 1.1.1.375Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.375NAD+ the enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate 389520
Show all pathways known for 1.1.1.375Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.375NADH NADPH is the preferred coenzyme 728317
Show all pathways known for 1.1.1.375Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.375NADH preference of NADP(H) over NAD(H).. The ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C. The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases 728123
Show all pathways known for 1.1.1.375Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.375NADH preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site 728123
Show all pathways known for 1.1.1.375Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.375NADH the enzyme prefers NADPH over NADH in reduction of oxaloacetate 389520
Show all pathways known for 1.1.1.375Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.375NADP+ preference of NADP(H) over NAD(H). The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases 728123
Show all pathways known for 1.1.1.375Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.375NADP+ the enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate 389520
Show all pathways known for 1.1.1.375Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.375NADPH NADPH is the preferred coenzyme 728317
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