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2.1.1.127: [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase

This is an abbreviated version!
For detailed information about [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.127

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

Synonyms

LSMT, LSMT-L, Methyltransferase, ribulose diphosphate carboxylase large subunit(lysine), More, PKMT, protein lysine methyltransferase, protein-lysine methyltransferase, protein-lysine methyltransferase-like, rbcMT, Ribulose 1,5-bisphosphate carboxylase/oxygenase large subunit Nepsilon-methyltransferase, Ribulose bisphosphate carboxylase large subunit methyltransferase, Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilonN-methyltransferase, Ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase, RLSMT, Rubisco large subunit epsilonN-methyltransferase, Rubisco large subunit methyltransferase, Rubisco large-subunit dimethyltransferase, Rubisco LS methyltransferase, Rubisco LSMT, Rubisco methyltransferase, SET-domain protein lysine methyltransferase, [Ribulose-bisphosphate-carboxylase]-lysine N-methyltransferase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.127 [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase

Crystallization

Crystallization on EC 2.1.1.127 - [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with S-adenosyl-L-homocysteine, hanging drop method, 25°C, reservoir solution contains HEPES 100 mM, pH 6.8, sodium acetate 1.2-1.35 M, structure analysis
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enzyme in complex with S-adenosyl-L-methionine, crystal structure analysis
-
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