23S rRNK (adenin2085-N6)-dimetiltransferaza
23S rRNK (adenin2085-N6)-dimetiltransferaza (EC 2.1.1.184, ErmC' metiltransferaza, ermC metilaza, ermC 23S rRNK metiltransferaza, rRNK:m6A metiltransferaza ErmC' , ErmC' , rRNK metiltransferaza ErmC' ) je enzim sa sistematskim imenom S-adenozil-L-metionin:23S rRNK (adenin2085-N6)-dimetiltransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
23S rRNK (adenin2085-N6)-dimetiltransferaza | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifikatori | |||||||||
EC broj | 2.1.1.184 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
|
- 2 S-adenozil-L-metionin + adenin2085 u 23S rRNK 2 S-adenozil-L-homocistein + N6-dimetiladenin2085 u 23S rRNK
ErmC je metiltransferaza koja pruža otpornost na makrolid-linkozamid-streptograminsku B grupu antibiotika tako što katalizuje metilaciju 23S rRNK na adeninu2085.
Reference uredi
- ↑ Zhong, P., Pratt, S.D., Edalji, R.P., Walter, K.A., Holzman, T.F., Shivakumar, A.G. and Katz, L. (1995). „Substrate requirements for ErmC′ methyltransferase activity”. J. Bacteriol. 177: 4327-4332. PMID 7543473.
- ↑ Denoya, C. and Dubnau, D. (1989). „Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase”. J. Biol. Chem. 264: 2615-2624. PMID 2492520.
- ↑ Denoya, C.D. and Dubnau, D. (1987). „Site and substrate specificity of the ermC 23S rRNA methyltransferase”. J. Bacteriol. 169: 3857-3860. PMID 2440853.
- ↑ Bussiere, D.E., Muchmore, S.W., Dealwis, C.G., Schluckebier, G., Nienaber, V.L., Edalji, R.P., Walter, K.A., Ladror, U.S., Holzman, T.F. and Abad-Zapatero, C. (1998). „Crystal structure of ErmC′, an rRNA methyltransferase which mediates antibiotic resistance in bacteria”. Biochemistry 37: 7103-7112. PMID 9585521.
- ↑ Schluckebier, G., Zhong, P., Stewart, K.D., Kavanaugh, T.J. and Abad-Zapatero, C. (1999). „The 2.2 Å structure of the rRNA methyltransferase ErmC′ and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism”. J. Mol. Biol. 289: 277-291. PMID 10366505.
- ↑ Maravic, G., Bujnicki, J.M., Feder, M., Pongor, S. and Flogel, M. (2003). „Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC′ redefines the substrate-binding site and suggests a model for protein-RNA interactions”. Nucleic Acids Res. 31: 4941-4949. PMID 12907737.
Literatura uredi
- 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.