(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
Pretraga PMC articles PubMed articles NCBI Protein search

(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 ${\displaystyle \rightleftharpoons }$ 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

1. 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. 
2. 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. 
3. 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. 
4. 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. 
5. 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

• 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. 

Vanjske veze

• MeSH (ribulose-bisphosphate+carboxylase)-lysine+N-methyltransferase