ExplorEnz: EC 2.1.1.127

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2.1.1.127

Accepted name:

[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase

Reaction:

3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N⁶,N⁶,N⁶-trimethyl-L-lysine

Other name(s):

rubisco methyltransferase; ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase; ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit εN-methyltransferase; S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase; RuBisCO methyltransferase; RuBisCO LSMT

Systematic name:

S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine N⁶-methyltransferase

Comments:

The enzyme catalyses three successive methylations of Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39). Only the three methylated form is observed [3]. The enzyme from pea (Pisum sativum) also three-methylates a specific lysine in the chloroplastic isoforms of fructose-bisphosphate aldolase (EC 4.1.2.13) [5].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 139171-98-5

References:

1.	Wang, P., Royer, M., Houtz, R.L. Affinity purification of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit ^εN-methyltransferase. Protein Expr. Purif. 6 (1995) 528–536. [DOI] [PMID: 8527940]
2.	Ying, Z., Janney, N., Houtz, R.L. Organization and characterization of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit N-methyltransferase gene in tobacco. Plant Mol. Biol. 32 (1996) 663–672. [PMID: 8980518]
3.	Dirk, L.M., Flynn, E.M., Dietzel, K., Couture, J.F., Trievel, R.C. and Houtz, R.L. Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases. Biochemistry 46 (2007) 3905–3915. [DOI] [PMID: 17338551]
4.	Magnani, R., Nayak, N.R., Mazarei, M., Dirk, L.M. and Houtz, R.L. Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase. J. Biol. Chem. 282 (2007) 27857–27864. [DOI] [PMID: 17635932]
5.	Mininno, M., Brugiere, S., Pautre, V., Gilgen, A., Ma, S., Ferro, M., Tardif, M., Alban, C. and Ravanel, S. Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants. J. Biol. Chem. 287 (2012) 21034–21044. [DOI] [PMID: 22547063]

[EC 2.1.1.127 created 1999, modified 2012]