16S rRNA (adenine1408-N1)-methyltransferase

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16S rRNA (adenine1408-N1)-methyltransferase
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EC no. 2.1.1.180
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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. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + adenine 1408 in 16S rRNA S-adenosyl-L-homocysteine + N1-methyladenine 1408 in 16S rRNA

The enzyme provides a panaminoglycoside resistance through interference with the binding of aminoglycosides.

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.

mRNA (guanine-N7-)-methyltransferase Enzyme

In enzymology, a mRNA (guanine-N7-)-methyltransferase also known as mRNA cap guanine-N7 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 tRNA (adenine-N1-)-methyltransferase (EC 2.1.1.36) 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

16S rRNA (guanine527-N7)-methyltransferase (EC 2.1.1.170, ribosomal RNA small subunit methyltransferase G, 16S rRNA methyltransferase RsmG, GidB, rsmG (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine527-N7)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (cytosine967-C5)-methyltransferase (EC 2.1.1.176, rsmB (gene), fmu (gene), 16S rRNA m5C967 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytosine967-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (cytosine1407-C5)-methyltransferase (EC 2.1.1.178, RNA m5C methyltransferase YebU, RsmF, YebU) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytosine1407-C5)-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 (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

tRNA (cytidine56-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (cytidine56-2'-O)-methyltransferase. 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

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

16S rRNA (guanine1516-N2)-methyltransferase (EC 2.1.1.242, yhiQ (gene), rsmJ (gene), m2G1516 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine1516-N2)-methyltransferase. This enzyme catalyses the following chemical reaction

References

  1. Beauclerk AA, Cundliffe E (February 1987). "Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides". Journal of Molecular Biology. 193 (4): 661–71. doi:10.1016/0022-2836(87)90349-4. PMID   2441068.
  2. Koscinski L, Feder M, Bujnicki JM (May 2007). "Identification of a missing sequence and functionally important residues of 16S rRNA:m(1)A1408 methyltransferase KamB that causes bacterial resistance to aminoglycoside antibiotics". Cell Cycle. 6 (10): 1268–71. doi: 10.4161/cc.6.10.4231 . PMID   17495534.
  3. Holmes DJ, Drocourt D, Tiraby G, Cundliffe E (June 1991). "Cloning of an aminoglycoside-resistance-encoding gene, kamC, from Saccharopolyspora hirsuta: comparison with kamB from Streptomyces tenebrarius". Gene. 102 (1): 19–26. doi:10.1016/0378-1119(91)90532-g. PMID   1840536.
  4. Wachino J, Shibayama K, Kurokawa H, Kimura K, Yamane K, Suzuki S, Shibata N, Ike Y, Arakawa Y (December 2007). "Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides". Antimicrobial Agents and Chemotherapy. 51 (12): 4401–9. doi:10.1128/aac.00926-07. PMC   2168023 . PMID   17875999.