(Formate-C-acetyltransferase)-activating enzyme and Radical SAM

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

Difference between (Formate-C-acetyltransferase)-activating enzyme and Radical SAM

(Formate-C-acetyltransferase)-activating enzyme vs. Radical SAM

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. Radical SAM is a designation for a superfamily of enzymes that use a + cluster to reductively cleave S-adenosyl-L-methionine (SAM) to generate a radical, usually a 5′-deoxyadenosyl radical, as a critical intermediate.

Similarities between (Formate-C-acetyltransferase)-activating enzyme and Radical SAM

(Formate-C-acetyltransferase)-activating enzyme and Radical SAM have 1 thing in common (in Unionpedia): S-Adenosyl methionine.

S-Adenosyl methionine

S-Adenosyl methionineSAM-e, SAMe, SAM, S-Adenosyl-L-methionine, AdoMet, ademetionine is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation.

(Formate-C-acetyltransferase)-activating enzyme and S-Adenosyl methionine · Radical SAM and S-Adenosyl methionine · See more »

The list above answers the following questions

What (Formate-C-acetyltransferase)-activating enzyme and Radical SAM have in common
What are the similarities between (Formate-C-acetyltransferase)-activating enzyme and Radical SAM

(Formate-C-acetyltransferase)-activating enzyme and Radical SAM Comparison

(Formate-C-acetyltransferase)-activating enzyme has 13 relations, while Radical SAM has 36. As they have in common 1, the Jaccard index is 2.04% = 1 / (13 + 36).

References

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

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