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Literature summary for 2.1.1.127 extracted from

  • Trievel, R.C.; Beach, B.M.; Dirk, L.M.A.; Houtz, R.L.; Hurley, J.H.
    Structure and catalytic mechanism of a SET domain protein methyltransferase (2002), Cell, 111, 91-103.
    View publication on PubMed
Search for more literature for 2.1.1.127

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli BL21, His-tagged protein Pisum sativum

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Pisum sativum

Inhibitors

Inhibitors Comment Organism Structure
S-adenosyl-L-homocysteine
-
 Pisum sativum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pisum sativum histone methylation has significant effects on heterochromatin formation and transcriptional regulation ?
-
 ?
S-adenosyl-L-methionine + histone L-lysine Pisum sativum
-
 S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
 ?

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from E. coli Pisum sativum

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine catalytic mechanism Pisum sativum
a
S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine substrate and inhibitor binding site Pisum sativum
a
S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine amino acid sequence comparison Pisum sativum
a
S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine enzyme is encoded on genes containing the SET-domain sequence, substrate specificity is connected to SET sequence Pisum sativum
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information histone methylation has significant effects on heterochromatin formation and transcriptional regulation Pisum sativum ?
-
 ?
S-adenosyl-L-methionine + histone L-lysine
-
 Pisum sativum S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Pisum sativum