Multisite-specific tRNA:(cytosine-C5)-methyltransferase

Multisite-specific tRNA:(cytosine-C5)-methyltransferase (EC 2.1.1.202, multisite-specific tRNA:m5C-methyltransferase, TRM4 (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytosine-C5)-methyltransferase.^[1]^[2]^[3]^[4] This enzyme catalyses the following chemical reaction

(1) S-adenosyl-L-methionine + cytosine³⁴ in tRNA precursor

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S-adenosyl-L-homocysteine + 5-methylcytosine³⁴ in tRNA precursor

(2) S-adenosyl-L-methionine + cytosine⁴⁰ in tRNA precursor

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S-adenosyl-L-homocysteine + 5-methylcytosine⁴⁰ in tRNA precursor

(3) S-adenosyl-L-methionine + cytosine⁴⁸ in tRNA

\rightleftharpoons

S-adenosyl-L-homocysteine + 5-methylcytosine⁴⁸ in tRNA

(4) S-adenosyl-L-methionine + cytosine⁴⁹ in tRNA

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S-adenosyl-L-homocysteine + 5-methylcytosine⁴⁹ in tRNA

The enzyme from Saccharomyces cerevisiae is responsible for complete 5-methylcytosine methylations of yeast tRNA.

References

↑ Motorin, Y. and Grosjean, H. (1999). "Multisite-specific tRNA:m5C-methyltransferase (Trm4) in yeast Saccharomyces cerevisiae: identification of the gene and substrate specificity of the enzyme". RNA 5: 1105–1118. doi:10.1017/s1355838299982201. PMID 10445884.
↑ Jiang, H.Q., Motorin, Y., Jin, Y.X. and Grosjean, H. (1997). "Pleiotropic effects of intron removal on base modification pattern of yeast tRNA^Phe: an in vitro study". Nucleic Acids Res. 25: 2694–2701. doi:10.1093/nar/25.14.2694. PMID 9207014.
↑ Strobel, M.C. and Abelson, J. (1986). "Effect of intron mutations on processing and function of Saccharomyces cerevisiae SUP53 tRNA in vitro and in vivo". Mol. Cell. Biol. 6: 2663–2673. doi:10.1128/mcb.6.7.2663. PMID 3537724.
↑ Walbott, H., Husson, C., Auxilien, S. and Golinelli-Pimpaneau, B. (2007). "Cysteine of sequence motif VI is essential for nucleophilic catalysis by yeast tRNA m⁵C methyltransferase". RNA 13: 967–973. doi:10.1261/rna.515707. PMID 17475914.

External links

Multisite-specific tRNA:(cytosine-C5)-methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)

Transferase: one carbon transferases (EC 2.1)

2.1.1: Methyl-

N-	Histamine N-methyltransferase Phenylethanolamine N-methyltransferase Amine N-methyltransferase Phosphatidylethanolamine N-methyltransferase

O-	5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase Catechol-O-methyl transferase

Homocysteine	Betaine-homocysteine methyltransferase Homocysteine methyltransferase Methionine synthase

Other	Phosphatidyl ethanolamine methyltransferase DNMT3B Histone methyltransferase Thymidylate synthase DNA methyltransferase Thiopurine methyltransferase

2.1.2: Hydroxymethyl-,
Formyl- and Related

Hydroxymethyltransferase	Serine hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase

Formyltransferase	Phosphoribosylglycinamide formyltransferase Inosine monophosphate synthase

Other	Glutamate formimidoyltransferase Aminomethyltransferase

2.1.3: Carboxy-
and Carbamoyl

Carboxy	methylmalonyl-CoA carboxytransferase

Carbamoyl	Aspartate carbamoyltransferase Ornithine carbamoyltransferase Oxamate carbamoyltransferase Putrescine carbamoyltransferase 3-hydroxymethylcephem carbamoyltransferase Lysine carbamoyltransferase N-acetylornithine carbamoyltransferase

2.1.4: Amidine

Arginine:glycine amidinotransferase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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