(Ribuloza-bisfosfat karboksilaza)-lizin N-metiltransferaza
| (Ribuloza-bisfosfat karboksilaza)-lizin N-metiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.1.127 | ||||||||
| CAS broj | 139171-98-5 | ||||||||
| 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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(Ribuloza-bisfosfat karboksilaza)-lizin N-metiltransferaza (EC 2.1.1.127, rubiska metiltransferaza, ribuloza-bisfosfat-karboksilaza/oksigenaza N-metiltransferaza, ribuloza-1,5-bisfosfat karboksilaza/oksigenaza velika podjedinica epsilon N-metiltransferaza, S-adenozil-L-metionin:(3-fosfo-D-glicerat-karboksi-lijaza (dimerizacija))-lizin 6-N-metiltransferaza, RuBisCO metiltransferaza, RuBisCO LSMT) je enzim sa sistematskim imenom S-adenozil-L-metionin:(3-fosfo-D-glicerat-karboksi-lijaza (dimerizacija))-lizin N6-metiltransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 3 S-adenozil-L-metionin + [ribuloza-1,5-bisfosfat karboksilaza]-L-lizin 3 S-adenozil-L-homocistein + [ribuloza-1,5-bisfosfat karboksilaza]-N6,N6,N6-trimetil-L-lizin
Ovaj enzim katalizuje tri sukcesivne metilacije Lys-14 u velikoj podjedinici heksadecamerne ribuloza-bisfosfat-karboksilaze (EC 4.1.1.39) kod viših biljaka.
Reference[uredi | uredi kod]
- ↑ Wang, P., Royer, M., Houtz, R.L. (1995). „Affinity purification of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit εN-methyltransferase”. Protein Expr. Purif. 6: 528-536. PMID 8527940.
- ↑ Ying, Z., Janney, N., Houtz, R.L. (1996). „Organization and characterization of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit N-methyltransferase gene in tobacco”. Plant Mol. Biol. 32: 663-672. PMID 8980518.
- ↑ Dirk, L.M., Flynn, E.M., Dietzel, K., Couture, J.F., Trievel, R.C. and Houtz, R.L. (2007). „Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases”. Biochemistry 46: 3905-3915. PMID 17338551.
- ↑ Magnani, R., Nayak, N.R., Mazarei, M., Dirk, L.M. and Houtz, R.L. (2007). „Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase”. J. Biol. Chem. 282: 27857-27864. PMID 17635932.
- ↑ Mininno, M., Brugiere, S., Pautre, V., Gilgen, A., Ma, S., Ferro, M., Tardif, M., Alban, C. and Ravanel, S. (2012). „Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants”. J. Biol. Chem. 287: 21034-21044. PMID 22547063.
Literatura[uredi | uredi kod]
- 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.
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- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.