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Literature summary extracted from

  • Trievel, R.C.; Flynn, E.M.; Houtz, R.L.; Hurley, J.H.
    Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT (2003), Nat. Struct. Biol., 10, 545-552.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.127 hanging drop vapour diffusion method, the crystal structure of the large subunit of the enzyme in ternary complex with either Lys or epsilon-N-methyllysine and the product S-adenosylhomocysteine are determined to resolution of 2.65 and 2.55 A, respectively Pisum sativum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.127 Lys
-
 Pisum sativum
2.1.1.127 methyl-L-Lys
-
 Pisum sativum

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.127 Pisum sativum Q43088
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.127 S-adenosyl-L-methionine + L-Lys
-
 Pisum sativum S-adenosyl-L-homocysteine + methyl-L-Lys
-
 ?
2.1.1.127 S-adenosyl-L-methionine + methyl-L-Lys about 2fold higher activity than with Lys Pisum sativum S-adenosyl-L-homocysteine + dimethyl-L-Lys + trimethyl-L-Lys
-
 ?
2.1.1.127 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-lysine
-
 Pisum sativum S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.127 LSMT
-
 Pisum sativum
2.1.1.127 Rubisco LSMT
-
 Pisum sativum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.127 0.000062
-
 L-Lys
-
 Pisum sativum
2.1.1.127 0.00025
-
 methyl-L-Lys
-
 Pisum sativum

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.1.127 37
-
 L-Lys
-
 Pisum sativum
2.1.1.127 101
-
 methyl-L-Lys
-
 Pisum sativum