23S rRNA (guanine745-N1)-methyltransferase

23S rRNA (guanine⁷⁴⁵-N¹)-methyltransferase (EC 2.1.1.187, Rlma(I), Rlma1, 23S rRNA m1G745 methyltransferase, YebH, RlmAI methyltransferase, ribosomal RNA(m1G)-methylase, rRNA(m1G)methylase, RrmA, 23S rRNA:m1G745 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine⁷⁴⁵-N¹)-methyltransferase.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + guanine⁷⁴⁵ in 23S rRNA

\rightleftharpoons

S-adenosyl-L-homocysteine + N¹-methylguanine⁷⁴⁵ in 23S rRNA

The enzyme specifically methylates guanine⁷⁴⁵ at N¹ in 23S rRNA.

References

↑ Liu, M., Novotny, G.W. and Douthwaite, S. (2004). "Methylation of 23S rRNA nucleotide G⁷⁴⁵ is a secondary function of the RlmA^I methyltransferase". RNA 10: 1713–1720. doi:10.1261/rna.7820104. PMID 15388872.
↑ Gustafsson, C. and Persson, B.C. (1998). "Identification of the rrmA gene encoding the 23S rRNA m¹G⁷⁴⁵ methyltransferase in Escherichia coli and characterization of an m¹G⁷⁴⁵-deficient mutant". J. Bacteriol. 180: 359–365. PMID 9440525.
↑ Das, K., Acton, T., Chiang, Y., Shih, L., Arnold, E. and Montelione, G.T. (2004). "Crystal structure of RlmA^I: implications for understanding the 23S rRNA G⁷⁴⁵/G⁷⁴⁸-methylation at the macrolide antibiotic-binding site". Proc. Natl. Acad. Sci. USA 101: 4041–4046. doi:10.1073/pnas.0400189101. PMID 14999102.
↑ Hansen, L.H., Kirpekar, F. and Douthwaite, S. (2001). "Recognition of nucleotide G⁷⁴⁵ in 23 S ribosomal RNA by the rrmA methyltransferase". J. Mol. Biol. 310: 1001–1010. doi:10.1006/jmbi.2001.4836. PMID 11501991.
↑ Liu, M. and Douthwaite, S. (2002). "Methylation at nucleotide G⁷⁴⁵ or G⁷⁴⁸ in 23S rRNA distinguishes Gram-negative from Gram-positive bacteria". Mol. Microbiol. 44: 195–204. doi:10.1046/j.1365-2958.2002.02866.x. PMID 11967079.

External links

23S rRNA (guanine745-N1)-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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