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Literature summary for 2.1.1.127 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
Search for more literature for 2.1.1.127

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
Lys
-
 Pisum sativum
methyl-L-Lys
-
 Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum Q43088
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + L-Lys
-
 Pisum sativum S-adenosyl-L-homocysteine + methyl-L-Lys
-
 ?
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
-
 ?
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

Synonyms Comment Organism
LSMT
-
 Pisum sativum
Rubisco LSMT
-
 Pisum sativum

Turnover Number [1/s]

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

Ki Value [mM]

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