TRNA-uridine aminocarboxypropyltransferase

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tRNA-uridine aminocarboxypropyltransferase
Identifiers
EC no. 2.5.1.25
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BRENDA BRENDA entry
ExPASy NiceZyme view
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MetaCyc metabolic pathway
PRIAM profile
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In enzymology, a tRNA-uridine aminocarboxypropyltransferase (EC 2.5.1.25) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + tRNA uridine 5'-methylthioadenosine + tRNA 3-(3-amino-3-carboxypropyl)-uridine

Thus, the two substrates of this enzyme are S-adenosyl-L-methionine and tRNA uridine, whereas its two products are 5'-methylthioadenosine and tRNA 3-(3-amino-3-carboxypropyl)-uridine.

This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA-uridine 3-(3-amino-3-carboxypropyl)transferase.

Related Research Articles

<i>S</i>-Adenosyl methionine Chemical compound found in all domains of life with largely unexplored effects

S-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. Although these anabolic reactions occur throughout the body, most SAM is produced and consumed in the liver. More than 40 methyl transfers from SAM are known, to various substrates such as nucleic acids, proteins, lipids and secondary metabolites. It is made from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase. SAM was first discovered by Giulio Cantoni in 1952.

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References


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