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Ligand a [histone H3]-N6-methyl-L-lysine27

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.356

S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27

755068, 754534, 754061, 753497, 754369, 754730, 755242, 755533

-

2.1.1.356

S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine27

755536

-

2.1.1.356

2 entries

2.1.1.371

S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine27

755933

-

In Vivo Product in Enzyme-catalyzed Reactions (6 results)

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Show Natural Product (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.65

[histone H3]-N6,N6-dimethyl-L-lysine27 + 2-oxoglutarate + O2 = [histone H3]-N6-methyl-L-lysine27 + succinate + formaldehyde + CO2

-

-

1.14.11.68

[histone H3]-N6,N6-dimethyl-L-lysine 27 + 2-oxoglutarate + O2 = [histone H3]-N6-methyl-L-lysine 27 + succinate + formaldehyde + CO2

-

-

2.1.1.356

S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27

-

-

2.1.1.356

S-adenosyl-L-methionine + [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27

-

-

2.1.1.356

2 entries

2.1.1.369

S-adenosyl-L-methionine + [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27

-

-

2.1.1.371

S-adenosyl-L-methionine + [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27

-

-

Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.356

S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27

755068, 754534, 754061, 753497, 754369, 754730, 755242, 755533

-

2.1.1.356

S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine27

755536

-

2.1.1.371

S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine27

758007

-

2.1.1.371

S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine27 = S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine27

755933

-

2.1.1.356

2 entries

2.1.1.371

2 entries

Product in Enzyme-catalyzed Reactions (9 results)

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Show Product (9 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.65

[histone H3]-N6,N6-dimethyl-L-lysine27 + 2-oxoglutarate + O2 = [histone H3]-N6-methyl-L-lysine27 + succinate + formaldehyde + CO2

-

-

1.14.11.68

a [histone H3]-N6,N6,N6-trimethyl-L-lysine27 + 2 2-oxoglutarate + 2 O2 = a [histone H3]-N6-methyl-L-lysine27 + 2 succinate + 2 formaldehyde + 2 CO2

-

-

1.14.11.68

a [histone H3]-N6,N6-dimethyl-L-lysine27 + 2-oxoglutarate + O2 = a [histone H3]-N6-methyl-L-lysine27 + succinate + formaldehyde + CO2

-

-

1.14.11.68

[histone H3]-N6,N6-dimethyl-L-lysine 27 + 2-oxoglutarate + O2 = [histone H3]-N6-methyl-L-lysine 27 + succinate + formaldehyde + CO2

-

-

2.1.1.356

S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27

-

-

2.1.1.356

S-adenosyl-L-methionine + [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27

-

-

1.14.11.68

3 entries

2.1.1.356

2 entries

2.1.1.369

S-adenosyl-L-methionine + [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27

-

-

2.1.1.371

S-adenosyl-L-methionine + a [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine27

-

-

2.1.1.371

S-adenosyl-L-methionine + [histone H3]-L-lysine27 = S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine27

-

-

2.1.1.371

2 entries

Enzyme Kinetic Parameters

References & Links

Literature References (11)

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Show Reference (11 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

753497

21070394

MiR-138 inhibits EZH2 methyltransferase expression and methylation of histone H3 at lysine 27, and affects thermotolerance acquisition

2011

Kisliouk, T.; Yosefi, S.; Meiri, N.

Eur. J. Neurosci.

33

224-235

754061

11316813

Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3

2001

Tachibana, M.; Sugimoto, K.; Fukushima, T.; Shinkai, Y.

J. Biol. Chem.

276

25309-25317

754369

21958314

Structure-guided design of a methyl donor cofactor that controls a viral histone H3 lysine 27 methyltransferase activity

2011

Li, J.; Wei, H.; Zhou, M.M.

J. Med. Chem.

54

7734-7738

754534

21715480

Epigenetic silencing of HIV-1 by the histone H3 lysine 27 methyltransferase enhancer of Zeste 2

2011

Friedman, J.; Cho, W.K.; Chu, C.K.; Keedy, K.S.; Archin, N.M.; Margolis, D.M.; Karn, J.

J. Virol.

85

9078-9089

754730

25047840

Polycomb repressive complex 2 and H3K27me3 cooperate with H3K9 methylation to maintain heterochromatin protein 1alpha at chromatin

2014

Boros, J.; Arnoult, N.; Stroobant, V.; Collet, J.F.; Decottignies, A.

Mol. Cell. Biol.

34

3662-3674

755068

24204317

The Fusarium graminearum histone H3 K27 methyltransferase KMT6 regulates development and expression of secondary metabolite gene clusters

2013

Connolly, L.R.; Smith, K.M.; Freitag, M.

PLoS Genet.

9

e1003916

755242

22323599

Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27)

2012

McCabe, M.T.; Graves, A.P.; Ganji, G.; Diaz, E.; Halsey, W.S.; Jiang, Y.; Smitheman, K.N.; Ott, H.M.; Pappalardi, M.B.; Allen, K.E.; Chen, S.B.; Della Pietra, A.; Dul, E.; Hughes, A.M.; Gilbert, S.A.; Thrall, S.H.; Tummino, P.J.; Kruger, R.G.; Brandt, M.; Schwartz, B.; Creasy, C.L.

Proc. Natl. Acad. Sci. USA

109

2989-2994

755533

12351676

Role of histone H3 lysine 27 methylation in polycomb-group silencing

2002

Cao, R.; Wang, L.; Wang, H.; Xia, L.; Erdjument-Bromage, H.; Tempst, P.; Jones, R.; Zhang, Y.

Science

298

1039-1043

755536

26472914

Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2

2015

Jiao, L.; Liu, X.

Science

350

aac4383

755933

16682010

Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity

2006

Kim, S.M.; Kee, H.J.; Eom, G.H.; Choe, N.W.; Kim, J.Y.; Kim, Y.S.; Kim, S.K.; Kook, H.; Kook, H.; Seo, S.B.

Biochem. Biophys. Res. Commun.

345

318-323

758007

15546353

Molecular characterization of the tobacco SET domain protein NtSET1 unravels its role in histone methylation, chromatin binding, and segregation

2004

Yu, Y.; Dong, A.; Shen, W.H

Plant J.

40

699-711

Links to other databases for a [histone H3]-N6-methyl-L-lysine27

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Show Links (1 entry)