Glycerol-3-phosphate dehydrogenase and NADH:ubiquinone oxidoreductase (H+-translocating)

Shortcuts: Differences, Similarities, Jaccard Similarity Coefficient, References.

Difference between Glycerol-3-phosphate dehydrogenase and NADH:ubiquinone oxidoreductase (H+-translocating)

Glycerol-3-phosphate dehydrogenase vs. NADH:ubiquinone oxidoreductase (H+-translocating)

Glycerol-3-phosphate dehydrogenase (GPDH) is an enzyme that catalyzes the reversible redox conversion of dihydroxyacetone phosphate (a.k.a. glycerone phosphate, outdated) to sn-glycerol 3-phosphate. NADH:ubiquinone oxidoreductase (also referred to as Type I NADH dehydrogenase and mitochondrial Complex I especially in humans) is an enzyme of the respiratory chains of myriad organisms from bacteria to humans.

Similarities between Glycerol-3-phosphate dehydrogenase and NADH:ubiquinone oxidoreductase (H+-translocating)

Glycerol-3-phosphate dehydrogenase and NADH:ubiquinone oxidoreductase (H+-translocating) have 7 things in common (in Unionpedia): Cofactor (biochemistry), Electron transport chain, Enzyme, Flavin adenine dinucleotide, Metformin, Mitochondrion, Nicotinamide adenine dinucleotide.

Cofactor (biochemistry)

A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's activity.

Cofactor (biochemistry) and Glycerol-3-phosphate dehydrogenase · Cofactor (biochemistry) and NADH:ubiquinone oxidoreductase (H+-translocating) · See more »

Electron transport chain

An electron transport chain (ETC) is a series of complexes that transfer electrons from electron donors to electron acceptors via redox (both reduction and oxidation occurring simultaneously) reactions, and couples this electron transfer with the transfer of protons (H+ ions) across a membrane.

Electron transport chain and Glycerol-3-phosphate dehydrogenase · Electron transport chain and NADH:ubiquinone oxidoreductase (H+-translocating) · See more »

Enzyme

Enzymes are macromolecular biological catalysts.

Enzyme and Glycerol-3-phosphate dehydrogenase · Enzyme and NADH:ubiquinone oxidoreductase (H+-translocating) · See more »

Flavin adenine dinucleotide

In biochemistry, flavin adenine dinucleotide (FAD) is a redox cofactor, more specifically a prosthetic group of a protein, involved in several important enzymatic reactions in metabolism.

Flavin adenine dinucleotide and Glycerol-3-phosphate dehydrogenase · Flavin adenine dinucleotide and NADH:ubiquinone oxidoreductase (H+-translocating) · See more »

Metformin

Metformin, marketed under the trade name Glucophage among others, is the first-line medication for the treatment of type 2 diabetes, particularly in people who are overweight.

Glycerol-3-phosphate dehydrogenase and Metformin · Metformin and NADH:ubiquinone oxidoreductase (H+-translocating) · See more »

Mitochondrion

The mitochondrion (plural mitochondria) is a double-membrane-bound organelle found in most eukaryotic organisms.

Glycerol-3-phosphate dehydrogenase and Mitochondrion · Mitochondrion and NADH:ubiquinone oxidoreductase (H+-translocating) · See more »

Nicotinamide adenine dinucleotide

Nicotinamide adenine dinucleotide (NAD) is a coenzyme found in all living cells.

Glycerol-3-phosphate dehydrogenase and Nicotinamide adenine dinucleotide · NADH:ubiquinone oxidoreductase (H+-translocating) and Nicotinamide adenine dinucleotide · See more »

The list above answers the following questions

What Glycerol-3-phosphate dehydrogenase and NADH:ubiquinone oxidoreductase (H+-translocating) have in common
What are the similarities between Glycerol-3-phosphate dehydrogenase and NADH:ubiquinone oxidoreductase (H+-translocating)

Glycerol-3-phosphate dehydrogenase and NADH:ubiquinone oxidoreductase (H+-translocating) Comparison

Glycerol-3-phosphate dehydrogenase has 42 relations, while NADH:ubiquinone oxidoreductase (H+-translocating) has 123. As they have in common 7, the Jaccard index is 4.24% = 7 / (42 + 123).

References

This article shows the relationship between Glycerol-3-phosphate dehydrogenase and NADH:ubiquinone oxidoreductase (H+-translocating). To access each article from which the information was extracted, please visit:

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