Get it on Google Play
New! Download Unionpedia on your Android™ device!
Faster access than browser!

(Formate-C-acetyltransferase)-activating enzyme and Oxidoreductase

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

Difference between (Formate-C-acetyltransferase)-activating enzyme and Oxidoreductase

(Formate-C-acetyltransferase)-activating enzyme vs. Oxidoreductase

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. 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 (Formate-C-acetyltransferase)-activating enzyme and Oxidoreductase

(Formate-C-acetyltransferase)-activating enzyme and Oxidoreductase have 2 things in common (in Unionpedia): Enzyme, List of enzymes.


Enzymes are macromolecular biological catalysts.

(Formate-C-acetyltransferase)-activating enzyme and Enzyme · 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.

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

The list above answers the following questions

(Formate-C-acetyltransferase)-activating enzyme and Oxidoreductase Comparison

(Formate-C-acetyltransferase)-activating enzyme has 13 relations, while Oxidoreductase has 35. As they have in common 2, the Jaccard index is 4.17% = 2 / (13 + 35).


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

Hey! We are on Facebook now! »