ExplorEnz: EC 2.1.1.180

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2.1.1.180

Accepted name:

16S rRNA (adenine¹⁴⁰⁸-N¹)-methyltransferase

Reaction:

S-adenosyl-L-methionine + adenine¹⁴⁰⁸ in 16S rRNA = S-adenosyl-L-homocysteine + N¹-methyladenine¹⁴⁰⁸ in 16S rRNA

Other name(s):

kanamycin-apramycin resistance methylase; 16S rRNA:m¹A¹⁴⁰⁸ methyltransferase; KamB; NpmA; 16S rRNA m¹A¹⁴⁰⁸ methyltransferase

Systematic name:

S-adenosyl-L-methionine:16S rRNA (adenine¹⁴⁰⁸-N¹)-methyltransferase

Comments:

The enzyme provides a panaminoglycoside-resistant nature through interference with the binding of aminoglycosides toward the A site of 16S rRNA through N¹-methylation at position adenine¹⁴⁰⁸ [4].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Beauclerk, A.A. and Cundliffe, E. Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides. J. Mol. Biol. 193 (1987) 661–671. [DOI] [PMID: 2441068]
2.	Koscinski, L., Feder, M. and Bujnicki, J.M. Identification of a missing sequence and functionally important residues of 16S rRNA:m¹A¹⁴⁰⁸ methyltransferase KamB that causes bacterial resistance to aminoglycoside antibiotics. Cell Cycle 6 (2007) 1268–1271. [DOI] [PMID: 17495534]
3.	Holmes, D.J., Drocourt, D., Tiraby, G. and Cundliffe, E. Cloning of an aminoglycoside-resistance-encoding gene, kamC, from Saccharopolyspora hirsuta: comparison with kamB from Streptomyces tenebrarius. Gene 102 (1991) 19–26. [DOI] [PMID: 1840536]
4.	Wachino, J., Shibayama, K., Kurokawa, H., Kimura, K., Yamane, K., Suzuki, S., Shibata, N., Ike, Y. and Arakawa, Y. Novel plasmid-mediated 16S rRNA m¹A¹⁴⁰⁸ methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides. Antimicrob. Agents Chemother. 51 (2007) 4401–4409. [DOI] [PMID: 17875999]

[EC 2.1.1.180 created 2010]