2.1.1.125: histone-arginine N-methyltransferase
This is an abbreviated version!
For detailed information about histone-arginine N-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.125
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2.1.1.125
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chromatin
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epigenetic
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trimethylation
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blow
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prmts
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deacetylase
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leukemia
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polycomb
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heterochromatin
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zeste
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oncogenic
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dimethylarginine
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sound
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dolphin
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acoustic
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demethylase
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vocal
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ribonucleoproteins
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nucleosomes
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monomethylation
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h3k4me3
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suv39h1
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hypomethylated
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telomeres
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trithorax
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euchromatic
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spliceosomal
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corepressors
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dimethylaminohydrolase
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chromatin-modifying
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nurses
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truncatus
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bottlenose
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histone-modifying
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suvar3-9
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mixed-lineage
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lys4
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fibrillarin
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sdmas
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medicine
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chromodomain
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tudor
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snrnp
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drug development
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s-adenosyl-l-homocysteine
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menin
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non-histone
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epigenome
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chromatin-remodeling
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chromatin-associated
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analysis
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dnmt3a
-
whale
- 2.1.1.125
- chromatin
-
epigenetic
-
trimethylation
-
blow
-
prmts
-
deacetylase
- leukemia
-
polycomb
- heterochromatin
-
zeste
-
oncogenic
- dimethylarginine
-
sound
- dolphin
-
acoustic
- demethylase
-
vocal
-
ribonucleoproteins
- nucleosomes
-
monomethylation
-
h3k4me3
- suv39h1
-
hypomethylated
-
telomeres
-
trithorax
-
euchromatic
-
spliceosomal
-
corepressors
-
dimethylaminohydrolase
-
chromatin-modifying
- nurses
- truncatus
-
bottlenose
-
histone-modifying
-
suvar3-9
-
mixed-lineage
- lys4
-
fibrillarin
-
sdmas
- medicine
-
chromodomain
-
tudor
-
snrnp
- drug development
- s-adenosyl-l-homocysteine
-
menin
-
non-histone
-
epigenome
-
chromatin-remodeling
-
chromatin-associated
- analysis
- dnmt3a
- whale
deleted, now covered by EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.320, type II protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase and EC 2.1.1.322, type IV protein arginine methyltransferase
ECTree
Advanced search results
Results in table 98 AA Sequence 5 Expression 30 General Information 38 kcat/KM [mM/s] 102 PDB ID
KCat KM Value
KCat KM Value on EC 2.1.1.125 - histone-arginine N-methyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
kcat/KM VALUE [1/mMs-1] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
6.6
N-acetyl-SFRGKGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
2.17
N-acetyl-SGmeRGKGGKGLGKGGAKRHRKV
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
14.3
N-acetyl-SGRGKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK
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at 30°C and pH 8.0
9.9
N-acetyl-SGRGRGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
26.7
N-acetyl-SGRme1GKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK
-
at 30°C and pH 8.0
0.15
WGGYSmeRGGYGGW
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
0.061
WGGYSRGGYGGW
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
additional information
additional information
-
Michaelis-Menten kinetics, kcat/Km for S-adenosyl-L-methionine is almost 2000fold higher for PRMT1 than for PRMT2, and the kcat/Km for histone H4 is nearly 600fold higher
-
0.013
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
mutant enzyme M48A, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
0.46
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
mutant enzyme M155A, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
1.7
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
mutant enzyme M48L, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
4.5
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
wild type enzyme, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
0.48
N-acetyl-SGRGKGGKGLGKGGAKRHRKV
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
7.3
N-acetyl-SGRGKGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
2.5
S-adenosyl-L-methionine
-
using N-acetyl-SGRGKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK as cosubstrate, at 30°C and pH 8.0
3.5
S-adenosyl-L-methionine
-
using N-acetyl-SGRme1GKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK as cosubstrate, at 30°C and pH 8.0
ECTree
2.1.1.125 histone-arginine N-methyltransferaseAdvanced search results
results (
results (| Results | in table |
|---|---|
| 98 | AA Sequence |
| 5 | Expression |
| 30 | General Information |
| 38 | kcat/KM [mM/s] |
| 102 | PDB ID |
KCat KM Value
KCat KM Value on EC 2.1.1.125 - histone-arginine N-methyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.6
N-acetyl-SFRGKGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
2.17
N-acetyl-SGmeRGKGGKGLGKGGAKRHRKV
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
14.3
N-acetyl-SGRGKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK
-
at 30°C and pH 8.0
9.9
N-acetyl-SGRGRGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
26.7
N-acetyl-SGRme1GKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK
-
at 30°C and pH 8.0
0.15
WGGYSmeRGGYGGW
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
0.061
WGGYSRGGYGGW
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
additional information
additional information
-
Michaelis-Menten kinetics, kcat/Km for S-adenosyl-L-methionine is almost 2000fold higher for PRMT1 than for PRMT2, and the kcat/Km for histone H4 is nearly 600fold higher
-
0.013
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
mutant enzyme M48A, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
0.46
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
mutant enzyme M155A, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
1.7
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
mutant enzyme M48L, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
4.5
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
wild type enzyme, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
0.48
N-acetyl-SGRGKGGKGLGKGGAKRHRKV
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
7.3
N-acetyl-SGRGKGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
2.5
S-adenosyl-L-methionine
-
using N-acetyl-SGRGKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK as cosubstrate, at 30°C and pH 8.0
3.5
S-adenosyl-L-methionine
-
using N-acetyl-SGRme1GKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK as cosubstrate, at 30°C and pH 8.0
