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Literature summary for 2.1.1.356 extracted from

  • Zhao, X.; Wang, Y.; Wang, Y.; Liu, Y.; Gao, S.
    Histone methyltransferase TXR1 is required for both H3 and H3.3 lysine 27 methylation in the well-known ciliated protist Tetrahymena thermophila (2017), Sci. China Life Sci., 60, 264-270 .
    View publication on PubMed
Search for more literature for 2.1.1.356

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27 Tetrahymena thermophila
-
 S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
 ?
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27 Tetrahymena thermophila SB210
-
 S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
 ?
S-adenosyl-L-methionine + [histone H3]-L-lysine27 Tetrahymena thermophila
-
 S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
 ?
S-adenosyl-L-methionine + [histone H3]-L-lysine27 Tetrahymena thermophila SB210
-
 S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
 ?

Organism

Organism UniProt Comment Textmining
Tetrahymena thermophila Q23QI3
-
-
Tetrahymena thermophila SB210 Q23QI3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
-
 Tetrahymena thermophila S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
 ?
S-adenosyl-L-methionine + [histone H3.3]-L-lysine27
-
 Tetrahymena thermophila SB210 S-adenosyl-L-homocysteine + [histone H3.3]-N6-methyl-L-lysine27
-
 ?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
-
 Tetrahymena thermophila S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
 ?
S-adenosyl-L-methionine + [histone H3]-L-lysine27
-
 Tetrahymena thermophila SB210 S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27
-
 ?

Synonyms

Synonyms Comment Organism
TXR1
-
 Tetrahymena thermophila

General Information

General Information Comment Organism
physiological function the enzyme affects DNA replication elongation in Tetrahymena thermophila Tetrahymena thermophila