23S rRNA (guanine745-N1)-methyltransferase

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23S rRNA (guanine745-N1)-methyltransferase
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EC no. 2.1.1.187
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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 + guanine 745 in 23S rRNA S-adenosyl-L-homocysteine + N1-methylguanine 745 in 23S rRNA

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

Related Research Articles

<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.

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

23S rRNA (uridine2552-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uridine2552-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (pseudouridine1915-N3)-methyltransferase (EC 2.1.1.177, YbeA, RlmH, pseudouridine methyltransferase, m3Psi methyltransferase, Psi1915-specific methyltransferase, rRNA large subunit methyltransferase H) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (pseudouridine1915-N3)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (guanine1405-N7)-methyltransferase (EC 2.1.1.179, methyltransferase Sgm, m7G1405 Mtase, Sgm Mtase, Sgm, sisomicin-gentamicin methyltransferase, sisomicin-gentamicin methylase, GrmA, RmtB, RmtC, ArmA) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine1405-N7)-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 (guanosine2251-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanosine2251-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (cytidine2498-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (cytidine2498-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine748-N1)-methyltransferase (EC 2.1.1.188, Rlma(II), Rlma2, 23S rRNA m1G748 methyltransferase, RlmaII, Rlma II, tylosin-resistance methyltransferase RlmA(II), TlrB, rRNA large subunit methyltransferase II) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine748-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (uracil1939-C5)-methyltransferase (EC 2.1.1.190, RumA, RNA uridine methyltransferase A, YgcA) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uracil1939-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (cytosine1962-C5)-methyltransferase (EC 2.1.1.191, RlmI, rRNA large subunit methyltransferase I, YccW) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (cytosine1962-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenine2503-C2)-methyltransferase (EC 2.1.1.192, RlmN, YfgB, Cfr) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C2)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenine2503-C2,C8)-dimethyltransferase (EC 2.1.1.194, Cfr, Cfr methyltransferase, Cfr rRNA methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C2,C8)-dimethyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine2535-N1)-methyltransferase (EC 2.1.1.209, AviRa) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine2535-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenine2503-C8)-methyltransferase (EC 2.1.1.224, Cfr (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C8)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (cytidine1920-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (cytidine1920-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenosine1067-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenosine1067-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine2069-N7)-methyltransferase (EC 2.1.1.264, rlmK (gene), 23S rRNA m7G2069 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine2069-N7)-methyltransferase. This enzyme catalyses the following chemical reaction

References

  1. Liu M, Novotny GW, Douthwaite S (November 2004). "Methylation of 23S rRNA nucleotide G745 is a secondary function of the RlmAI methyltransferase". RNA. 10 (11): 1713–20. doi:10.1261/rna.7820104. PMC   1370659 . PMID   15388872.
  2. Gustafsson C, Persson BC (January 1998). "Identification of the rrmA gene encoding the 23S rRNA m1G745 methyltransferase in Escherichia coli and characterization of an m1G745-deficient mutant". Journal of Bacteriology. 180 (2): 359–65. doi:10.1128/JB.180.2.359-365.1998. PMC   106891 . PMID   9440525.
  3. Das K, Acton T, Chiang Y, Shih L, Arnold E, Montelione GT (March 2004). "Crystal structure of RlmAI: implications for understanding the 23S rRNA G745/G748-methylation at the macrolide antibiotic-binding site". Proceedings of the National Academy of Sciences of the United States of America. 101 (12): 4041–6. Bibcode:2004PNAS..101.4041D. doi: 10.1073/pnas.0400189101 . PMC   384692 . PMID   14999102.
  4. Hansen LH, Kirpekar F, Douthwaite S (July 2001). "Recognition of nucleotide G745 in 23 S ribosomal RNA by the rrmA methyltransferase". Journal of Molecular Biology. 310 (5): 1001–10. doi:10.1006/jmbi.2001.4836. PMID   11501991.
  5. Liu M, Douthwaite S (April 2002). "Methylation at nucleotide G745 or G748 in 23S rRNA distinguishes Gram-negative from Gram-positive bacteria". Molecular Microbiology. 44 (1): 195–204. doi: 10.1046/j.1365-2958.2002.02866.x . PMID   11967079.