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N-acetylhexosamine 1-dehydrogenase and Oxidoreductase

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

Difference between N-acetylhexosamine 1-dehydrogenase and Oxidoreductase

N-acetylhexosamine 1-dehydrogenase vs. Oxidoreductase

In enzymology, a N-acetylhexosamine 1-dehydrogenase is an enzyme that catalyzes the chemical reaction Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine and NAD+, whereas its 3 products are N-acetyl-D-glucosaminate, NADH, and H+. In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor.

Similarities between N-acetylhexosamine 1-dehydrogenase and Oxidoreductase

N-acetylhexosamine 1-dehydrogenase and Oxidoreductase have 3 things in common (in Unionpedia): Enzyme, List of enzymes, Nicotinamide adenine dinucleotide.

Enzyme

Enzymes are macromolecular biological catalysts.

Enzyme and N-acetylhexosamine 1-dehydrogenase · Enzyme and Oxidoreductase · See more »

List of enzymes

This page lists enzymes by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission numbering system.

List of enzymes and N-acetylhexosamine 1-dehydrogenase · List of enzymes and Oxidoreductase · See more »

Nicotinamide adenine dinucleotide

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

N-acetylhexosamine 1-dehydrogenase and Nicotinamide adenine dinucleotide · Nicotinamide adenine dinucleotide and Oxidoreductase · See more »

The list above answers the following questions

N-acetylhexosamine 1-dehydrogenase and Oxidoreductase Comparison

N-acetylhexosamine 1-dehydrogenase has 10 relations, while Oxidoreductase has 35. As they have in common 3, the Jaccard index is 6.67% = 3 / (10 + 35).

References

This article shows the relationship between N-acetylhexosamine 1-dehydrogenase and Oxidoreductase. To access each article from which the information was extracted, please visit:

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