TRNA (adenine-N6-)-methyltransferase

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tRNA (adenine-N6-)-methyltransferase
Identifiers
EC no. 2.1.1.55
CAS no. 9014-53-3
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MetaCyc metabolic pathway
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In enzymology, a tRNA (adenine-N6-)-methyltransferase (EC 2.1.1.55) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + tRNA S-adenosyl-L-homocysteine + tRNA containing N6-methyladenine

Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA, whereas its two products are S-adenosylhomocysteine and tRNA containing N6-methyladenine.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (adenine-N6-)-methyltransferase. This enzyme is also called S-adenosyl-L-methionine:tRNA (adenine-6-N-)-methyltransferase.

Related Research Articles

<span class="mw-page-title-main">DNA methyltransferase</span> Class of enzymes

In biochemistry, the DNA methyltransferase family of enzymes catalyze the transfer of a methyl group to DNA. DNA methylation serves a wide variety of biological functions. All the known DNA methyltransferases use S-adenosyl methionine (SAM) as the methyl donor.

<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.

<span class="mw-page-title-main">Methyltransferase</span> Group of methylating enzymes

Methyltransferases are a large group of enzymes that all methylate their substrates but can be split into several subclasses based on their structural features. The most common class of methyltransferases is class I, all of which contain a Rossmann fold for binding S-Adenosyl methionine (SAM). Class II methyltransferases contain a SET domain, which are exemplified by SET domain histone methyltransferases, and class III methyltransferases, which are membrane associated. Methyltransferases can also be grouped as different types utilizing different substrates in methyl transfer reactions. These types include protein methyltransferases, DNA/RNA methyltransferases, natural product methyltransferases, and non-SAM dependent methyltransferases. SAM is the classical methyl donor for methyltransferases, however, examples of other methyl donors are seen in nature. The general mechanism for methyl transfer is a SN2-like nucleophilic attack where the methionine sulfur serves as the leaving group and the methyl group attached to it acts as the electrophile that transfers the methyl group to the enzyme substrate. SAM is converted to S-Adenosyl homocysteine (SAH) during this process. The breaking of the SAM-methyl bond and the formation of the substrate-methyl bond happen nearly simultaneously. These enzymatic reactions are found in many pathways and are implicated in genetic diseases, cancer, and metabolic diseases. Another type of methyl transfer is the radical S-Adenosyl methionine (SAM) which is the methylation of unactivated carbon atoms in primary metabolites, proteins, lipids, and RNA.

<span class="mw-page-title-main">DNA adenine methylase</span> Prokaryotic enzyme

DNA adenine methylase, (Dam methylase) (also site-specific DNA-methyltransferase (adenine-specific), EC 2.1.1.72, modification methylase, restriction-modification system) is an enzyme that adds a methyl group to the adenine of the sequence 5'-GATC-3' in newly synthesized DNA. Immediately after DNA synthesis, the daughter strand remains unmethylated for a short time. It is an orphan methyltransferase that is not part of a restriction-modification system and regulates gene expression. This enzyme catalyses the following chemical reaction

In enzymology, a [cytochrome c]-lysine N-methyltransferase (EC 2.1.1.59) is an enzyme that catalyzes the chemical reaction

In enzymology, a mRNA (2'-O-methyladenosine-N6-)-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a rRNA (adenine-N6-)-methyltransferase (EC 2.1.1.48) is an enzyme that catalyzes the chemical reaction

In enzymology, a rRNA (guanine-N1-)-methyltransferase (EC 2.1.1.51) is an enzyme that catalyzes the chemical reaction

In enzymology, a rRNA (guanine-N2-)-methyltransferase (EC 2.1.1.52) is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (adenine-N1-)-methyltransferase (EC 2.1.1.36) is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (cytosine-5-)-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (guanine-N1-)-methyltransferase (EC 2.1.1.31) is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (guanine-N2-)-methyltransferase (EC 2.1.1.32) is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (guanine-N7-)-methyltransferase (EC 2.1.1.33) is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (uracil-5-)-methyltransferase is an enzyme that catalyzes the chemical reaction

23S rRNA (adenine1618-N6)-methyltransferase (EC 2.1.1.181, rRNA large subunit methyltransferase F, YbiN protein, rlmF (gene), m6A1618 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine1618-N6)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase (EC 2.1.1.182, S-adenosylmethionine-6-N',N'-adenosyl (rRNA) dimethyltransferase, KsgA, ksgA methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenine2085-N6)-dimethyltransferase (EC 2.1.1.184, ErmC' methyltransferase, ermC methylase, ermC 23S rRNA methyltransferase, rRNA:m6A methyltransferase ErmC', ErmC', rRNA methyltransferase ErmC' ) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2085-N6)-dimethyltransferase. This enzyme catalyses the following chemical reaction

TRNA1Val (adenine37-N6)-methyltransferase (EC 2.1.1.223, YfiC) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA1Val (adenine37-N6)-methyltransferase. This enzyme catalyses the following chemical reaction

References