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Literature summary extracted from

  • Mininno, M.; Brugiere, S.; Pautre, V.; Gilgen, A.; Ma, S.; Ferro, M.; Tardif, M.; Alban, C.; Ravanel, S.
    Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants (2012), J. Biol. Chem., 287, 21034-21044.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.127 expressed in Escherichia coli Rosetta-2 cells Pisum sativum
2.1.1.127 expressed in Escherichia coli Rosetta-2 cells Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.127 S-adenosyl-L-homocysteine
-
 Arabidopsis thaliana
2.1.1.127 S-adenosyl-L-homocysteine
-
 Pisum sativum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.127 0.0045
-
 [large subunit of Rubisco]-L-lysine at pH 7.8 and 30°C Pisum sativum
2.1.1.127 0.0129
-
 [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine at pH 7.8 and 30°C Pisum sativum
2.1.1.127 0.0138
-
 [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine at pH 7.8 and 30°C Arabidopsis thaliana
2.1.1.127 0.014
-
 [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine at pH 7.8 and 30°C Pisum sativum
2.1.1.127 0.0148
-
 [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine at pH 7.8 and 30°C Arabidopsis thaliana
2.1.1.127 0.314
-
 [gamma-tocopherol methyltransferase]-L-lysine at pH 7.8 and 30°C Arabidopsis thaliana
2.1.1.127 0.32
-
 [gamma-tocopherol methyltransferase]-L-lysine at pH 7.8 and 30°C Pisum sativum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.2.13 chloroplast
-
 Arabidopsis thaliana 9507
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.127 54600
-
 x * 54600, calculated from amino acid sequence Pisum sativum
2.1.1.127 54600
-
 x * 54600, calculated from amino acid sequence Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.127 additional information Arabidopsis thaliana in Arabidopsis, the large subunit of Rubisco is not naturally methylated. LSMT-L is able to interact with unmethylated Rubisco, but the complex is catalytically unproductive ?
-
 ?
2.1.1.127 S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-L-lysine Pisum sativum
-
 S-adenosyl-L-homocysteine [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine Pisum sativum
-
 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine Arabidopsis thaliana
-
 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine Pisum sativum
-
 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine Arabidopsis thaliana
-
 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-L-lysine Arabidopsis thaliana
-
 S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [large subunit of Rubisco]-L-lysine Pisum sativum methylation occurs at Lys-394 S-adenosyl-L-homocysteine + [large subunit of Rubisco]-N6-methyl-L-lysine
-
 ?
2.1.1.259 S-adenosyl-L-methionine + [fructose 1,6-bisphosphate aldolase]-L-lysine Arabidopsis thaliana the substrate is trimethylated at a conserved lysyl residue located close to the C terminus S-adenosyl-L-homocysteine + [fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.127 Arabidopsis thaliana
-
 ecotype Col-0
-
2.1.1.127 Pisum sativum
-
 cultivar Douce Provence
-
2.1.1.259 Arabidopsis thaliana
-
-
-
4.1.2.13 Arabidopsis thaliana
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.127 nickel-Sepharose column chromatography, Sephadex G-25 gel filtration, and Q-Sepharose column chromatography Pisum sativum
2.1.1.127 nickel-Sepharose column chromatography, Sephadex G-25 gel filtration, and Q-Sepharose column chromatography Arabidopsis thaliana

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.127 leaf
-
 Pisum sativum
-
2.1.1.127 leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.127 additional information in Arabidopsis, the large subunit of Rubisco is not naturally methylated. LSMT-L is able to interact with unmethylated Rubisco, but the complex is catalytically unproductive Arabidopsis thaliana ?
-
 ?
2.1.1.127 S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-L-lysine
-
 Pisum sativum S-adenosyl-L-homocysteine [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
-
 Pisum sativum S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
-
 Arabidopsis thaliana S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
-
 Pisum sativum S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
-
 Arabidopsis thaliana S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-L-lysine
-
 Arabidopsis thaliana S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [large subunit of Rubisco]-L-lysine methylation occurs at Lys-394 Pisum sativum S-adenosyl-L-homocysteine + [large subunit of Rubisco]-N6-methyl-L-lysine
-
 ?
2.1.1.259 S-adenosyl-L-methionine + [fructose 1,6-bisphosphate aldolase]-L-lysine the substrate is trimethylated at a conserved lysyl residue located close to the C terminus Arabidopsis thaliana S-adenosyl-L-homocysteine + [fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
-
 ?
2.1.1.259 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit]-L-lysine no natural substrate. The enzyme is able to interact with unmethylated Rubisco, but the complex is catalytically unproductive Arabidopsis thaliana S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit]-N6,N6,N6-trimethyl-L-lysine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.127 ? x * 54600, calculated from amino acid sequence Pisum sativum
2.1.1.127 ? x * 54600, calculated from amino acid sequence Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
2.1.1.127 LSMT
-
 Pisum sativum
2.1.1.127 LSMT-L
-
 Arabidopsis thaliana
2.1.1.127 protein-lysine methyltransferase
-
 Pisum sativum
2.1.1.127 protein-lysine methyltransferase-like
-
 Arabidopsis thaliana
2.1.1.259 LSMT-L
-
 Arabidopsis thaliana
2.1.1.259 protein-lysine methyltransferase-like
-
 Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
4.1.2.13 metabolism chloroplastic fructose 1,6-bisphosphate aldolase isoforms are methylated by protein-lysine methyltransferase LSMT. Trimethylation occurs at a conserved lysyl residue located close to the C terminus. Trimethylation does not modify the kinetic properties and tetrameric organization of the aldolases in vitro Arabidopsis thaliana

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.1.1.127 0.033
-
 [gamma-tocopherol methyltransferase]-L-lysine at pH 7.8 and 30°C Arabidopsis thaliana
2.1.1.127 0.05
-
 [gamma-tocopherol methyltransferase]-L-lysine at pH 7.8 and 30°C Pisum sativum
2.1.1.127 0.57
-
 [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine at pH 7.8 and 30°C Pisum sativum
2.1.1.127 0.933
-
 [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine at pH 7.8 and 30°C Arabidopsis thaliana
2.1.1.127 1.05
-
 [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine at pH 7.8 and 30°C Arabidopsis thaliana
2.1.1.127 1.05
-
 [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine at pH 7.8 and 30°C Pisum sativum
2.1.1.127 1.32
-
 [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine at pH 7.8 and 30°C Pisum sativum
2.1.1.127 8.65
-
 [large subunit of Rubisco]-L-lysine at pH 7.8 and 30°C Pisum sativum