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

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

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

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

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. Methionine (symbol Met or M) is an essential amino acid in humans.

Similarities between (Formate-C-acetyltransferase)-activating enzyme and Methionine

(Formate-C-acetyltransferase)-activating enzyme and Methionine have 2 things in common (in Unionpedia): Radical SAM, S-Adenosyl methionine.

Radical SAM

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.

(Formate-C-acetyltransferase)-activating enzyme and Radical SAM · Methionine and Radical SAM · See more »

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 · Methionine and S-Adenosyl methionine · See more »

The list above answers the following questions

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

(Formate-C-acetyltransferase)-activating enzyme has 13 relations, while Methionine has 126. As they have in common 2, the Jaccard index is 1.44% = 2 / (13 + 126).

References

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

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