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Literature summary for 2.1.1.355 extracted from

  • Chin, H.G.; Pradhan, M.; Esteve, P.O.; Patnaik, D.; Evans, T.C.; Pradhan, S.
    Sequence specificity and role of proximal amino acids of the histone H3 tail on catalysis of murine G9A lysine 9 histone H3 methyltransferase (2005), Biochemistry, 44, 12998-13006.
    View publication on PubMed
Search for more literature for 2.1.1.355

Application

Application Comment Organism
analysis sequence context of modified residue affects G9a activity and modification in the proximal amino acids influences methylation Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00017
-
 histone H3(K27A) recombinant substrate Mus musculus
0.00023
-
 histone H3(K4A) recombinant substrate Mus musculus
0.00026
-
 histone H3 recombinant substrate Mus musculus
0.0006
-
 histone K4-trimethylK9
-
 Mus musculus
0.0006
-
 histone H3 (T11phos) wild-type substrate Mus musculus
0.0009
-
 histone H3 wild-type substrate Mus musculus
0.0011
-
 histone H3 (1-13) wild-type substrate Mus musculus
0.0015
-
 histone K4AK9
-
 Mus musculus
0.0022
-
 histone K4-acetylK9
-
 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information minimal substrate methylated by G9a contains seven amino acids (TARKSTG) of the histone H3 tail Mus musculus ?
-
 ?
S-adenosyl-L-methionine + histone H3
-
 Mus musculus ?
-
 ?
S-adenosyl-L-methionine + histone H3 (1-13)
-
 Mus musculus ?
-
 ?
S-adenosyl-L-methionine + histone H3 (S10phos) phosphorylation of the proximal amino acids impairs Lys-9 methylation via impairing enzyme-substrate interaction Mus musculus ?
-
 ?
S-adenosyl-L-methionine + histone H3 (T11phos) phosphorylation of the proximal amino acids impairs Lys-9 methylation via impairing enzyme-substrate interaction Mus musculus ?
-
 ?
S-adenosyl-L-methionine + histone H3(K27A) mutation in the unstructured amino-terminal tail of histone H3 does not affect the central globular domain, but reduces the turnover numbers of the substrates Mus musculus ?
-
 ?
S-adenosyl-L-methionine + histone H3(K4A) mutation in the unstructured amino-terminal tail of histone H3 does not affect the central globular domain, but reduces the turnover numbers of the substrates Mus musculus ?
-
 ?
S-adenosyl-L-methionine + histone K4-acetylK9
-
 Mus musculus ?
-
 ?
S-adenosyl-L-methionine + histone K4-trimethylK9
-
 Mus musculus ?
-
 ?
S-adenosyl-L-methionine + histone K4AK9
-
 Mus musculus ?
-
 ?

Synonyms

Synonyms Comment Organism
G9a
-
 Mus musculus
G9a lysine 9 histone H3 methyltransferase
-
 Mus musculus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.001806
-
 histone H3 (S10phos) wild-type substrate Mus musculus
0.005
-
 histone H3 (T11phos) wild-type substrate Mus musculus
0.0089
-
 histone K4-acetylK9
-
 Mus musculus
0.0089
-
 histone K4-trimethylK9
-
 Mus musculus
0.01194
-
 histone K4AK9
-
 Mus musculus
0.0161
-
 histone H3(K4A) recombinant substrate Mus musculus
0.0161
-
 histone H3(K27A) recombinant substrate Mus musculus
0.02056
-
 histone H3 (1-13) wild-type substrate Mus musculus
0.02167
-
 histone H3 recombinant substrate Mus musculus
0.024
-
 histone H3 wild-type substrate Mus musculus