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Literature summary extracted from

  • Magnani, R.; Nayak, N.R.; Mazarei, M.; Dirk, L.M.; Houtz, R.L.
    Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase (2007), J. Biol. Chem., 282, 27857-27864.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.259 0.01923
-
 S-adenosyl-L-methionine in 100 mM Bicine, 20 mM MgCl2 pH 8.0, at 30°C Pisum sativum
2.1.1.259 1.2
-
 [large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-L-lysine in 100 mM Bicine, 20 mM MgCl2 pH 8.0, at 30°C Pisum sativum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.259 51700
-
 x * 51700, calculated from amino acid sequence Pisum sativum

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.259 Pisum sativum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.259 S-adenosyl-L-homocysteine + [large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-L-lysine mutagenesis of lysine residues 8, 18 and 28 to either Arg or Ala does not affect methylation of Lys-14 by the enzyme, whereas mutagenesis of the Lys-14 methylation site abolishes methylation Pisum sativum S-adenosyl-L-homocysteine + [large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-N6,N6,N6-trimethyl-L-lysine
-
 ?
2.1.1.259 S-adenosyl-L-methionine + [acyl carrier protein I precursor]-L-lysine
-
 Pisum sativum S-adenosyl-L-homocysteine + [acyl carrier protein I precursor]-N6,N6,N6-trimethyl-L-lysine
-
 ?
2.1.1.259 S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-L-lysine
-
 Pisum sativum S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6,N6,N6-trimethyl-L-lysine
-
 ?
2.1.1.259 S-adenosyl-L-methionine + [granule-bound starch synthase I precursor]-L-lysine
-
 Pisum sativum S-adenosyl-L-homocysteine + [granule-bound starch synthase I precursor]-N6,N6,N6-trimethyl-L-lysine
-
 ?
2.1.1.259 S-adenosyl-L-methionine + [NAD(P)H-quinone oxidoreductase chain 5]-L-lysine
-
 Pisum sativum S-adenosyl-L-homocysteine + [NAD(P)H-quinone oxidoreductase chain 5]-N6,N6,N6-trimethyl-L-lysine
-
 ?
2.1.1.259 S-adenosyl-L-methionine + [Rubisco large subunit]-L-lysine
-
 Pisum sativum S-adenosyl-L-homocysteine + [Rubisco large subunit]-N6,N6,N6-trimethyl-L-lysine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.259 ? x * 51700, calculated from amino acid sequence Pisum sativum

Synonyms

EC Number Synonyms Comment Organism
2.1.1.259 large subunit of Rubisco methyltransferase
-
 Pisum sativum
2.1.1.259 LSMT
-
 Pisum sativum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.259 0.011
-
 [large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-L-lysine in 100 mM Bicine, 20 mM MgCl2 pH 8.0, at 30°C Pisum sativum
2.1.1.259 0.019
-
 S-adenosyl-L-methionine in 100 mM Bicine, 20 mM MgCl2 pH 8.0, at 30°C Pisum sativum

General Information

EC Number General Information Comment Organism
2.1.1.259 malfunction knockdown of the LSMT homologue in transgenic tobacco plants results in a 2fold decrease of alpha-tocopherol Pisum sativum