2.1.1.356: [histone H3]-lysine27 N-trimethyltransferase
This is an abbreviated version!
For detailed information about [histone H3]-lysine27 N-trimethyltransferase, go to the full flat file.
Word Map on EC 2.1.1.356
-
2.1.1.356
-
chromatin
-
trimethylation
-
zeste
-
tumorigenesis
-
pluripotency
-
repressor
-
lncrnas
-
prc2-mediated
-
leukemia
-
heterochromatin
-
epigenome
-
ectoderm
-
methyltransferases
-
self-renewal
-
jarid2
-
bivalent
-
prc1
-
h3k4me3
-
nucleosome
-
imprint
-
cdkn2a
-
demethylase
-
dznep
-
vernalization
-
h3k27ac
-
ezh2-mediated
-
hotair
-
de-repression
-
3-deazaneplanocin
-
lysine-27
-
ctcf
-
jumonji
-
mescs
-
analysis
-
polycomb-group
-
curly
-
trithorax
-
homeotic
-
synthesis
-
mpnsts
-
polycomb-mediated
-
chromatin-modifying
- 2.1.1.356
- chromatin
-
trimethylation
-
zeste
- tumorigenesis
-
pluripotency
- repressor
- lncrnas
-
prc2-mediated
- leukemia
-
heterochromatin
-
epigenome
- ectoderm
- methyltransferases
-
self-renewal
- jarid2
-
bivalent
- prc1
-
h3k4me3
- nucleosome
-
imprint
-
cdkn2a
- demethylase
-
dznep
-
vernalization
-
h3k27ac
-
ezh2-mediated
-
hotair
-
de-repression
-
3-deazaneplanocin
-
lysine-27
- ctcf
-
jumonji
-
mescs
- analysis
-
polycomb-group
-
curly
-
trithorax
-
homeotic
- synthesis
- mpnsts
-
polycomb-mediated
-
chromatin-modifying
Reaction
3 S-adenosyl-L-methionine + = 3 S-adenosyl-L-homocysteine +
Synonyms
CLF, EC 2.1.1.43, EZH1, EZH2, G9a, histone H3 K27 methyltransferase, histone H3 lysine 27 methyltransferase, histone lysine methyltransferase, HMTase, interleukin-5 response element II binding protein, KMT6, KMT6A, KMT6B, lysine-preferring HMTase, NSD2, NSD3, Polycomb repressive complex 2, PRC2, RE-IIBP, SET, SET domain histone lysine methyltransferase, SETDB1, TXR1, vSET, WHSC1/MMSET isoform RE-IIBP
ECTree
Advanced search results
Engineering
Engineering on EC 2.1.1.356 - [histone H3]-lysine27 N-trimethyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
F679Y
A677G
the mutant cell line reveals aberrantly elevated trimethylated [histone H3]-L-lysine27 and decreased monomethylated and dimethylated [histone H3]-L-lysine27 as compared to the wild type. The mutant enzyme demonstrates nearly equal efficiency for all three substrates (unmethylated H3K27:monomethylated H3K27:dimethylated H3K27 kcat/Km ratio is 1.1:0.6:1)
C483A
-
no activity, the SET domain cysteine 483 is a critical residue for the histone methyltransferase activity of RE-IIBP
R477A
-
no activity, the SET domain 477 is a critical residue for the histone methyltransferase activity of RE-IIBP
F52Y
-
can only mono- and di- but not tri-methylate H38(K27)
L116A
the mutant shows strongly increased activity compared to the wild type enzyme
Y109G
the mutant shows strongly decreased activity compared to the wild type enzyme
Y50F
-
nearly abolishes di- and tri-methylation of H3(K27), but does not affect the mono-methylation
D329A
Thermochaetoides thermophila
-
the mutant shows strongly reduced activity compared to the wild type enzyme
DELTAL350
Thermochaetoides thermophila
-
the mutant shows strongly reduced activity compared to the wild type enzyme
H326A
Thermochaetoides thermophila
-
the mutant shows strongly reduced activity compared to the wild type enzyme
P325S
Thermochaetoides thermophila
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R839D
Thermochaetoides thermophila
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D329A
Thermochaetoides thermophila DSM1495
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
DELTAL350
Thermochaetoides thermophila DSM1495
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
H326A
Thermochaetoides thermophila DSM1495
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
P325S
Thermochaetoides thermophila DSM1495
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
R839D
Thermochaetoides thermophila DSM1495
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
additional information
-
the mutant is tolerated with about 2fold reduction compared with wild type
F679Y
-
the mutant retains the capacity to produce trimethylated histone H3(K27)
-
each SET domain mutation disrupts PRC2 histone methyltransferase, based on known SET domain structures, the mutations likely affect either the lysine-substrate binding pocket, the binding site for the adenosylmethionine methyl donor, or a critical tyrosine predicted to interact with the substrate lysine epsilon-amino group. The CXC mutant retains catalytic activity, Lys-27 specificity, and trimethylation capacity.
additional information
-
the E(z)Trm mutation increases the histone H3 (K27) trimethylation efficiency of catalytic subunit E(Z) of Polycomb Repressive Complex 2