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3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) and Oxidoreductase

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

Difference between 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) and Oxidoreductase

3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) vs. Oxidoreductase

In enzymology, a 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) is an enzyme that catalyzes the chemical reaction The 3 substrates of this enzyme are 3-methyl-2-oxobutanoate, CoA, and oxidized ferredoxin, whereas its 3 products are S-(2-methylpropanoyl)-CoA, CO2, and reduced ferredoxin. 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 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) and Oxidoreductase

3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) and Oxidoreductase have 2 things in common (in Unionpedia): Enzyme, List of enzymes.

Enzyme

Enzymes are proteins that act as biological catalysts by accelerating chemical reactions.

3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) and Enzyme · Enzyme and Oxidoreductase · See more »

List of enzymes

Enzymes are listed here by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system.

3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) and List of enzymes · List of enzymes and Oxidoreductase · See more »

The list above answers the following questions

3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) and Oxidoreductase Comparison

3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) has 10 relations, while Oxidoreductase has 46. As they have in common 2, the Jaccard index is 3.57% = 2 / (10 + 46).

References

This article shows the relationship between 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) and Oxidoreductase. To access each article from which the information was extracted, please visit: