23S rRNA (guanine2535-N1)-methyltransferase

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23S rRNA (guanine2535-N1)-methyltransferase
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EC no. 2.1.1.209
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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. [1] [2] [3] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + guanine 2535 in 23S rRNA S-adenosyl-L-homocysteine + N1-methylguanine2535 in 23S rRNA

This is one of the methyltransferases from Streptomyces viridochromogenes . Streptomyces viridochromogenes produces the antibiotic avilamycin A which binds to the 50S ribosomal subunit to inhibit protein synthesis. [4]

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.

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 (guanine2445-N2)-methyltransferase (EC 2.1.1.173, ycbY (gene), rlmL (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine2445-N2)-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 (adenine1408-N1)-methyltransferase (EC 2.1.1.180, kanamycin-apramycin resistance methylase, 16S rRNA:m1A1408 methyltransferase, KamB, NpmA, 16S rRNA m1A1408 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1408-N1)-methyltransferase. This enzyme catalyses the following 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

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

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. 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 (uracil747-C5)-methyltransferase (EC 2.1.1.189, YbjF, RumB, RNA uridine methyltransferase B) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uracil747-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,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 (uridine2479-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uridine2479-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (adenine22-N1)-methyltransferase (EC 2.1.1.217, TrmK, YqfN, Sp1610 (gene), tRNA: m1A22 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (adenine22-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (adenine58-N1)-methyltransferase (EC 2.1.1.220, tRNA m1A58 methyltransferase, tRNA (m1A58) methyltransferase, TrmI, tRNA (m1A58) Mtase, Rv2118cp, Gcd10p-Gcd14p, Trm61p-Trm6p) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (adenine58-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

16S rRNA (cytidine1409-2'-O)-methyltransferase (EC 2.1.1.227, TlyA) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytidine1409-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

tRNA (guanine37-N1)-methyltransferase (EC 2.1.1.228, TrmD, tRNA (m1G37) methyltransferase, transfer RNA (m1G37) methyltransferase, Trm5p, TRMT5, tRNA-(N1G37) methyltransferase, MJ0883 (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine37-N1)-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

References

  1. ↑ Treede I, Jakobsen L, Kirpekar F, Vester B, Weitnauer G, Bechthold A, Douthwaite S (July 2003). "The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA at the guanosine 2535 base and the uridine 2479 ribose". Molecular Microbiology. 49 (2): 309–18. doi: 10.1046/j.1365-2958.2003.03558.x . PMID   12828631.
  2. ↑ Weitnauer G, Gaisser S, Trefzer A, Stockert S, Westrich L, Quiros LM, Mendez C, Salas JA, Bechthold A (March 2001). "An ATP-binding cassette transporter and two rRNA methyltransferases are involved in resistance to avilamycin in the producer organism Streptomyces viridochromogenes Tü57". Antimicrobial Agents and Chemotherapy. 45 (3): 690–5. doi:10.1128/aac.45.3.690-695.2001. PMC   90357 . PMID   11181344.
  3. ↑ Mosbacher TG, Bechthold A, Schulz GE (May 2003). "Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes". Journal of Molecular Biology. 329 (1): 147–57. doi:10.1016/s0022-2836(03)00407-8. PMID   12742024.
  4. ↑ Krupkin M, Wekselman I, Matzov D, Eyal Z, Diskin Posner Y, Rozenberg H, Zimmerman E, Bashan A, Yonath A (November 2016). "Avilamycin and evernimicin induce structural changes in rProteins uL16 and CTC that enhance the inhibition of A-site tRNA binding". Proceedings of the National Academy of Sciences of the United States of America. 113 (44): E6796–E6805. doi: 10.1073/pnas.1614297113 . PMC   5098648 . PMID   27791159.
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