From Wikipedia, the free encyclopedia
16S rRNA (adenine1408-N1)-methyltransferase
Identifiers
EC no. 2.1.1.180
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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

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

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.

External links

From Wikipedia, the free encyclopedia
16S rRNA (adenine1408-N1)-methyltransferase
Identifiers
EC no. 2.1.1.180
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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

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

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.

External links


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