16S rRNK (adenin1518-N6/adenin1519-N6)-dimetiltransferaza
(Preusmjereno sa stranice KsgA)
16S rRNK (adenin1518-N6/adenin1519-N6)-dimetiltransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.1.1.182 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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16S rRNK (adenin1518-N6/adenin1519-N6)-dimetiltransferaza (EC 2.1.1.182, S-adenozilmetionin-6-N',N'-adenozil (rRNK) dimetiltransferaza, KsgA, ksgA metiltransferaza) je enzim sa sistematskim imenom S-adenozil-L-metionin:16S rRNK (adenin1518-N6/adenin1519-N6)-dimetiltransferaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 4 S-adenozil-L-metionin + adenin1518/adenin1519 u 16S rRNK 4 S-adenozil-L-homocistein + N6-dimetiladenin1518/N6-dimetiladenin1519 u 16S rRNK
KsgA proizvodi modifikaciju ribozomalne RNK koja je u najvećoj meri konzervirana, dimetilaciju adenina1518 i adenina1519 u 16S rRNK. Vrste koje nemaju ovu metilazu su otporne na kasugamicin.
- ↑ Helser, T.L., Davies, J.E. and Dahlberg, J.E. (1971). „Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli”. Nat. New Biol. 233: 12-14. PMID 4329247.
- ↑ Helser, T.L., Davies, J.E. and Dahlberg, J.E. (1972). „Mechanism of kasugamycin resistance in Escherichia coli”. Nat. New Biol. 235: 6-9. PMID 4336392.
- ↑ van Buul, C.P. and van Knippenberg, P.H. (1985). „Nucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNA”. Gene 38: 65-72. PMID 3905517.
- ↑ Formenoy, L.J., Cunningham, P.R., Nurse, K., Pleij, C.W. and Ofengand, J. (1994). „Methylation of the conserved A1518-A1519 in Escherichia coli 16S ribosomal RNA by the ksgA methyltransferase is influenced by methylations around the similarly conserved U1512.G1523 base pair in the 3′ terminal hairpin”. Biochimie 76: 1123-1128. PMID 7538324.
- ↑ O'Farrell, H.C., Scarsdale, J.N. and Rife, J.P. (2004). „Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli”. J. Mol. Biol. 339: 337-353. PMID 15136037.
- ↑ Poldermans, B., Roza, L. and Van Knippenberg, P.H. (1979). „Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3′ end of 16 S ribosomal RNA of Escherichia coli. III. Purification and properties of the methylating enzyme and methylase-30 S interactions”. J. Biol. Chem. 254: 9094-9100. PMID 383712.
- ↑ Demirci, H., Belardinelli, R., Seri, E., Gregory, S.T., Gualerzi, C., Dahlberg, A.E. and Jogl, G. (2009). „Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5′-methylthioadenosine”. J. Mol. Biol. 388: 271-282. PMID 19285505.
- ↑ Tu, C., Tropea, J.E., Austin, B.P., Court, D.L., Waugh, D.S. and Ji, X. (2009). „Structural basis for binding of RNA and cofactor by a KsgA methyltransferase”. Structure 17: 374-385. PMID 19278652.
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.