(Formate-C-acetyltransferase)-activating enzyme and List of enzymes

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

Difference between (Formate-C-acetyltransferase)-activating enzyme and List of enzymes

(Formate-C-acetyltransferase)-activating enzyme vs. List of enzymes

In enzymology, a -activating enzyme is an enzyme that catalyzes the chemical reaction The 3 substrates of this enzyme are S-adenosyl-L-methionine, dihydroflavodoxin, and formate C-acetyltransferase-glycine, whereas its 4 products are 5'-deoxyadenosine, L-methionine, flavodoxin semiquinone, and formate C-acetyltransferase-glycin-2-yl radical. This page lists enzymes by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission numbering system.

Similarities between (Formate-C-acetyltransferase)-activating enzyme and List of enzymes

(Formate-C-acetyltransferase)-activating enzyme and List of enzymes have 1 thing in common (in Unionpedia): Oxidoreductase.

Oxidoreductase

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.

(Formate-C-acetyltransferase)-activating enzyme and Oxidoreductase · List of enzymes and Oxidoreductase · See more »

The list above answers the following questions

What (Formate-C-acetyltransferase)-activating enzyme and List of enzymes have in common
What are the similarities between (Formate-C-acetyltransferase)-activating enzyme and List of enzymes

(Formate-C-acetyltransferase)-activating enzyme and List of enzymes Comparison

(Formate-C-acetyltransferase)-activating enzyme has 13 relations, while List of enzymes has 282. As they have in common 1, the Jaccard index is 0.34% = 1 / (13 + 282).

References

This article shows the relationship between (Formate-C-acetyltransferase)-activating enzyme and List of enzymes. To access each article from which the information was extracted, please visit:

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