16S rRNA (adenine1408-N1)-methyltransferase

16S rRNA (adenine-N)-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 (adenine-N)-methyltransferase. This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + adenine in 16S rRNA

\rightleftharpoons

S-adenosyl-L-homocysteine + N-methyladenine in 16S rRNA

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

References

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.
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.
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.
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.

External links

16S+rRNA+(adenine1408-N1)-methyltransferase at the U.S. 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 Cyclopropane-fatty-acyl-phospholipid synthase

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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 2.1.1