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Ligand histone

Basic Ligand Information

Molecular Structure

Related pathways

Show all BRENDA pathways known for histone

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (9 results)

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Show Natural Substrate (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.127

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

485354, 485355

-

2.1.1.354

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

485355

-

2.1.1.355

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

485355, 485353

-

2.1.1.360

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

703940

-

2.1.1.362

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

485352

-

2.3.1.48

acetyl-CoA + histone = CoA + acetyl-histone

704529, 705700, 703350

-

2.3.1.48

acetyl-CoA + histone = CoA + acetylhistone

487101, 487061, 487092, 487089, 487066, 487096, 487078, 487087, 659427, 658021, 704529, 705700, 702497, 735770, 736051

-

2.3.1.48

histone + acetyl-CoA = acetyl-histone + CoA

675799, 675963, 676627, 672263, 675618, 674735

-

2.3.1.48

3 entries

2.4.2.31

histone + NAD+ = Nomega-[(2'-phospho-ADP)-D-ribosyl]-histone-L-arginine + nicotinamide + H+

675027

-

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.98

N-acetyl-lysine-histone + H2O = acetate + histone

-

-

Substrate in Enzyme-catalyzed Reactions (35 results)

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Show Substrate (35 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.127

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

485354, 485355

-

2.1.1.354

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

485355

-

2.1.1.355

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

485355, 485353, 703442

-

2.1.1.360

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

703940

-

2.1.1.362

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

485352

-

2.1.1.364

S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine

702233, 720101

-

2.3.1.48

acetyl-CoA + histone = CoA + acetyl-histone

704529, 705700, 703350

-

2.3.1.48

acetyl-CoA + histone = CoA + acetylhistone

487101, 487078, 487098, 487095, 487096, 487100, 487072, 487077, 487097, 487091, 487092, 487093, 487099, 487071, 487073, 487075, 487080, 487083, 487063, 487085, 487094, 487089, 487076, 487081, 487090, 487062, 487066, 487061, 487079, 487065, 487059, 487087, 487069, 487067, 487070, 487068, 487060, 487082, 487088, 487086, 487074, 487084, 487064, 487102, 659427, 658021, 687924, 704529, 705700, 702497, 735770, 736051

-

2.3.1.48

histone + acetyl-CoA = acetyl-histone + CoA

675799, 675963, 676627, 672263, 675618, 674735

-

2.3.1.48

histone + propionyl-CoA = propionyl-histone + CoA

672263

-

2.3.1.48

4 entries

2.3.1.57

acetyl-CoA + histone = CoA + N-acetylhistone

487256

-

2.3.1.82

acetyl-CoA + histone = CoA + ?

636904

-

2.4.2.31

histone + NAD+ = nicotinamide + ?

638121, 638096, 638112, 657869

-

2.4.2.31

histone + NAD+ = Nomega-[(2'-phospho-ADP)-D-ribosyl]-histone-L-arginine + nicotinamide + H+

675027

-

2.4.2.31

2 entries

2.7.10.2

ATP + histone = ADP + phosphorylated histone

492030

-

2.7.11.1

ATP + histone = ADP + phosphorylated histone

532698, 660870, 661782, 663404, 680441, 723232, 721543, 762093

-

2.7.11.11

ATP + histone = ADP + phosphorylated histone

661884, 692294

-

2.7.11.12

ATP + histone = ADP + phosphorylated histone

662268

-

2.7.11.13

ATP + histone = ADP + phosphorylated histone

672833, 724130, 724170

-

2.7.11.17

ATP + histone = ?

490758, 490763, 490760, 490761

-

2.7.11.17

ATP + histone = ADP + phosphohistone

640685, 640689, 640688

-

2.7.11.17

2 entries

2.7.11.31

ATP + histone = ADP + phosphohistone

640764, 640765, 640767

-

2.7.12.1

ATP + histone = ADP + phosphorylated histone

532653

-

3.1.3.1

histone + H2O = ?

94563

-

3.1.3.16

histone + H2O = histone + phosphate

94873

-

3.1.3.17

histone + H2O = ?

94690

-

3.1.3.17

histone + H2O = phosphate + ?

94690

-

3.1.3.17

2 entries

3.4.21.103

histone + H2O = ?

647478

-

3.4.21.83

histone + H2O = ?

651697

-

3.4.21.B1

histone + H2O = ?

755588

-

3.4.22.1

histones + H2O = hydrolyzed histones

36638

-

3.4.22.15

histone + H2O = ?

647930

-

3.4.22.28

histone protein H3 + H2O = ?

648007

-

3.4.24.39

histone + H2O = ?

668858, 753029

-

3.4.24.39

Histone + H2O = Hydrolyzed histone

31238

-

3.4.24.39

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

1.5.3.4

N6-methyl-L-lysyl-histone + O2 + H2O = histone + formaldehyde + H2O2

-

-

3.1.1.61

methylated histones + H2O = histones + methanol

-

-

3.1.3.16

histone + H2O = histone + phosphate

-

-

3.1.3.16

phosphohistone + H2O = histone + phosphate

-

-

3.1.3.16

phosphorylated histone + H2O = histone + phosphate

-

-

3.1.3.16

3 entries

3.1.3.2

phosphotyrosyl histone + H2O = histone + phosphate

-

-

3.1.3.44

phosphohistone + H2O = histone + phosphate

-

-

3.5.1.98

acetylated histone + H2O = acetate + histone

-

-

3.5.1.98

N-acetyl-lysine-histone + H2O = acetate + histone

-

-

3.5.1.98

2 entries

Activator in Enzyme-catalyzed Reactions (17 results)

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Show Activating Compound (17 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.38

activation

489511

-

2.4.1.90

activation

489511

-

2.4.2.31

increases activity in absence of salt

638097

-

2.4.3.8

slight activation

639653

-

2.7.1.67

stimulates

641776

-

2.7.4.1

maximum activation in the presence of 20 mM phosphate

645114

-

2.7.4.1

required for activity

645112

-

2.7.4.1

strong inhibition of reverse reaction

645114

-

2.7.4.1

3 entries

2.8.2.17

stimulates, optimum concentration: 0.5 mg/ml

645747

-

2.8.2.5

stimulates, optimum concentration: 0.5 mg/ml

645747

-

3.1.3.16

-

134595, 134636, 134604

-

3.1.3.16

activation, depending on substrate

134620

-

3.1.4.11

activates

135131

-

3.1.4.11

maximal activation of hydrolysis of phosphatidylinositol 4,5-diphosphate at 0.0125 mg/ml

135136

-

3.1.3.16

2 entries

3.1.4.11

2 entries

3.1.4.3

PLC d1 and PLC d3

135282

-

3.4.21.B1

histones H1, H2A, H2B, H3, and H4 promote pro-plasma hyaluronan-binding protein autoactivation in vivo. Histones do not affect enzymatic activity of the active form of plasma hyaluronan-binding protein

717196

-

3.4.21.B1

the enzyme is activated by tissue injury, through the release of extracellular histones

776077

-

3.4.21.B1

2 entries

Inhibitor in Enzyme-catalyzed Reactions (13 results)

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Show Inhibitors (13 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.48

histone H1 acetylation is inhibited by all other histone fractions

487084

-

2.3.1.48

histones H2A, H2B, and H3

487078

-

2.3.1.48

inhibits spermidine acetylation, enzyme forms A and B

487064

-

2.3.1.48

3 entries

2.7.11.7

-

640777

-

2.7.4.1

reverse reaction, strong, activates forward reaction in the presence of phosphate

645114

-

3.1.3.16

competitive when glycogen synthase D is the substrate, increases the Km-value for glycogen synthase D 4fold, but shows mixed type inhibition when phosphorylase a acts as substrate with an 1.4fold increase of Km

655958

-

3.1.4.35

-

135351

-

3.2.1.143

-

208526

-

3.2.1.143

due to noncovalent interactions of the protein with free ADP-ribose polymers

208520

-

3.2.1.143

histone f2a, f2b and f3. Inhibition by histone f2a is reversed by DNA

208524

-

3.2.1.143

histone H1, H2A, H2B and H3

208528

-

3.2.1.143

histone H1, H2A, H2B, H3 and H4

208525

-

3.2.1.143

lysine-rich histone of calf thymus

208519

-

3.2.1.143

6 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (8 results)

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Show Turnover Number (8 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.3.1.48

0.0017

-

Rtt109

703350

2.3.1.48

0.0019

-

Esa1

703350

2.3.1.48

0.13

-

Rtt109 in complex with chaperone Vps75

703350

2.3.1.48

0.8

-

enzyme form type I

487067

2.3.1.48

1.6

-

Esa1 in piccolo NuA4-complex

703350

2.3.1.48

1.7

-

Gcn5

703350

2.3.1.48

12

-

enzyme form type II

487067

2.3.1.48

7 entries

3.1.3.17

3.3

-

-

94690

K_M Value (9 results)

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Show KM Value (9 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.1.48

0.075

-

Rtt109 in complex with chaperone Vps75

703350

2.3.1.48

0.083

-

Rtt109

703350

2.3.1.48

0.16

-

p300

703350

2.3.1.48

0.22

-

Esa1 in piccolo NuA4-complex with Yng2 and Epl1

703350

2.3.1.48

0.49

-

Gcn5

703350

2.3.1.48

1.4

-

Esa1

703350

2.3.1.48

6 entries

2.7.11.11

0.73

-

pH 7.0, 22°C, catalytic subunit

661884

2.7.11.31

0.005

-

-

640764

3.1.3.17

0.046

-

-

94690

References & Links

Literature References (140)

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Show Reference (140 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

31238

-

Neutral proteinases I and II of Aspergillus sojae. Action on various substrates.

1976

Sekine, H.

Agric. Biol. Chem.

40

703-709

36638

510307

Purification and properties of brain cathepsin B. Evidence for cleavage of pituitary lipotropins

1979

Suhar, A.; Marks, N.

Eur. J. Biochem.

101

23-30

94563

-

Alkaline phosphatase and its function as a protein phosphatase

1987

Stinson, R.A.; Chan, J.R.A.

Adv. Protein Phosphatases

4

127-151

94690

217307

Purification and properties of bovine myocardial phosphorylase phosphatase (protein phosphatase C)

1978

Killilea, S.D.; Aylward, J.H.; Mellgren, R.L.; Lee, E.Y.C.

Arch. Biochem. Biophys.

191

638-646

94873

4351138

Substrate specificity of glycogen synthase phosphatase from bovine heart: action on phosphorylase a and histone

1973

Nakai, C.; Thomas, J.A.

Biochem. Biophys. Res. Commun.

52

530-536

134595

-

Phosphoprotein phosphatases

1986

Ballou, L.M.; Fischer, E.H.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed.)

17

311-361

134604

-

Characterization of polycation-stimulated phosphoprotein phosphatase

1985

Schlender, K.K.; Wilson, S.E.; Thysseril, T.J.; Mellgren, R.L.

Adv. Protein Phosphatases

1

311-326

134620

-

Characterization of a high molecular weight phosphatase from rabbit reticulocytes

1987

Kramer, G.; Chen, S.C.; Wollny, E.; Hardesty, B.

Adv. Protein Phosphatases

4

269-292

134636

2985385

The protein phosphatases involved in cellular regulation. 2. Purification, subunit structure and properties of protein phosphatases-2A0, 2A1, and 2A2 from rabbit skeletal muscle

1985

Tung, H.Y.L.; Alemany, S.; Cohen, P.

Eur. J. Biochem.

148

253-263

135131

4284484

The triphosphoinositide phosphodiesterase of brain tissue

1964

Thompson, W.; Dawson, R.M.C.

Biochem. J.

91

237-243

135136

1646858

Purification, properties, and phosphorylation by protein kinase C of two phosphoinositidase C isoenzymes from rat brain

1991

Blank, J.L.; Foster, K.A.; Hawthorne, J.N.

J. Neurochem.

57

15-21

135282

9360711

Expression, purification and kinetic properties of human recombinant phospholipase C delta 3

1997

Pawelczyk, T.; Matecki, A.

Acta Biochim. Pol.

44

221-229

135351

-

Two-site high-affinity interaction between inhibitory and catalytic subunits of rod cyclic GMP phosphodiesterase

1992

Artemyev, N.O.; Hamm, H.E.

Biochem. J.

283

273-279

208519

-

Properties of poly(adenosine diphosphate ribose) polymerase, poly(adenosine diphosphate ribose) glycohydrolase and poly(adenosine diphosphate ribose)

1973

Sugimura, T.; Yamada, M.; Miwa, M.; Matsushima, T.; Hidaka, T.; Nagao, M.; Inui, N.; Takayama, S.

Biochem. Soc. Trans.

1

642-644

208520

10331632

Measurement of poly(ADP-ribose) glycohydrolase activity by high resolution polyacrylamide gel electrophoresis: specific inhibition by histones and nuclear matrix proteins

1999

Pacheco-Rodriguez, G.; Alvarez-Gonzalez, R.

Mol. Cell. Biochem.

193

13-18

208524

4831224

Purification and properties of a glycohydrolase from calf thymus splitting ribose-ribose linkages of poly(adenosine diphosphate ribose)

1974

Miwa, M.; Tanaka, M.; Matsushima, T.; Sugimura, T.

J. Biol. Chem.

249

3475-3482

208525

3771556

Purification and characterization of poly(ADP-ribose) glycohydrolase. Different modes of action on large and small poly(ADP-ribose)

1986

Hatakeyama, K.; Nemoto, Y.; Ueda, K.; Hayaishi, O.

J. Biol. Chem.

261

14902-14911

208526

3941108

Purification and properties of an (ADP-ribose)n glycohydrolase from guinea pig liver nuclei

1986

Tanuma, S.i.; Kawashima, K.; Endo, H.

J. Biol. Chem.

261

965-969

208528

6617643

Isolation and purification of poly(ADP-ribose) glycohydrolase from pig thymus

1983

Tavassoli, M.; Tavassoli, M.H.; Shall, S.

Eur. J. Biochem.

135

449-455

485352

12121615

Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase

2002

Fang, J.; Feng, Q.; Ketel, C.S.; Wang, H.; Cao, R.; Xia, L.; Erdjument-Bromage, H.; Tempst, P.; Simon, J.A.; Zhang, Y.

Curr. Biol.

12

1086-1099

485353

12130538

G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis

2002

Tachibana, M.; Sugimoto, K.; Nozaki, M.; Ueda, J.; Ohta, T.; Ohki, M.; Fukuda, M.; Takeda, N.; Niida, H.; Kato, H.; Shinkai, Y.

Genes Dev.

16

1779-1791

485354

12372303

Structure and catalytic mechanism of a SET domain protein methyltransferase

2002

Trievel, R.C.; Beach, B.M.; Dirk, L.M.A.; Houtz, R.L.; Hurley, J.H.

Cell

111

91-103

485355

12372294

Structures of SET domain proteins: protein lysine methyltransferases make their mark

2002

Yeates, T.O.

Cell

111

5-7

487059

5031160

Histone acetylation. Purification and properties of three histone-specific acetyltransferases from rat thymus nuclei

1972

Gallwitz, D.; Sures, I.

Biochim. Biophys. Acta

263

315-328

487060

22543

Calf liver nuclear N-acetyltransferases. Purification and properties of two enzymes with both spermidine acetyltransferase and histone acetyltransferase activities

1978

Libby, P.R.

J. Biol. Chem.

253

233-237

487061

7370043

Nucleosome-histone acetyltransferase from rat liver chromatin

1980

Fukushima, M.; Ota, K.; Fujimoto, D.; Horiuchi, K.

Biochem. Biophys. Res. Commun.

92

1409-1414

487062

-

A plant histone acetyltransferase specific for H3 in nucleosomes

1986

Sendra, R.; Salvador, M.L.; Lopez-Rodas, G.; Tordera, V.; Franco, L.

Plant Sci.

46

189-194

487063

-

On the ubiquitous presence of histone acetyltransferase B in eukaryotes

1985

Salvador, M.L.; Sendra, R.; Lopez-Rodas, G.; Tordera, V.; Franco, L.

FEBS Lett.

191

55-58

487064

7406506

Rat liver nuclear N-acetyltransferases: separation of two enzymes with both histone and spermidine acetyltransferase activity

1980

Libby, P.R.

Arch. Biochem. Biophys.

203

384-389

487065

3890750

Partial purification and properties of two histone acetyltransferases from the yeast, Saccharomyces cerevisiae

1985

Lopez-Rodas, G.; Perez-Ortin, J.E.; Tordera, V.; Salvador, M.L.; Franco, L.

Arch. Biochem. Biophys.

239

184-190

487066

1730297

Enzymes involved in the dynamic equilibrium of core histone acetylation of Physarum polycephalum

1992

Lopez-Rodas, G.; Brosch, G.; Golderer, G.; Lindner, H.; Grobner, P.; Loidl, P.

FEBS Lett.

296

82-86

487067

2303486

Purification and characterization of two porcine liver nuclear histone acetyltransferases

1990

Attisano, L.; Lewis, P.N.

J. Biol. Chem.

265

3949-3955

487068

6389549

Extensive purification and characterization of chromatin-bound histone acetyltransferase from Saccharomyces cerevisiae

1984

Travis, G.H.; Colavito-Shepanski, M.; Grunstein, M.

J. Biol. Chem.

259

14406-14412

487069

6736037

Two species of histone acetyltransferase in rat liver nuclei

1984

Yukioka, M.; Sasaki, S.; Qi, S.L.; Inoue, A.

J. Biol. Chem.

259

8372-8377

487070

6706965

Porcine liver nuclear histone acetyltransferase. Partial purification and basic properties

1984

Kelner, D.N.; McCarty, K.S.

J. Biol. Chem.

259

3413-3419

487071

7118937

Inhibition of histone acetylation by N-[2-(S-coenzyme A)acetyl] spermidine amide, a multisubstrate analog

1982

Cullis, P.M.; Wolfenden, R.; Cousens, L.S.; Alberts, B.M.

J. Biol. Chem.

257

12165-12169

487072

7225345

Substrate and product inhibition initial rate kinetics of histone acetyltransferase

1981

Wiktorowicz, J.E.; Campos, K.L.; Bonner, J.

Biochemistry

20

1464-1467

487073

7213362

Effect of sea urchin sperm chromatin on histone acetylation

1980

Wong, L.J.C.

Biochem. Biophys. Res. Commun.

97

1362-1369

487074

1772401

High-mobility group and other nonhistone substrates for nuclear histone N-acetyltransferase

1991

Wong, L.J.C.; Sharpe, D.J.; Wong, S.S.

Biochem. Genet.

29

461-475

487075

3996726

Salt inhibition of nuclear histone acetyltransferase from calf thymus

1985

Wong, L.J.; Patton, W.F.

Int. J. Biochem.

17

123-126

487076

6257509

A histone-specific acetyltransferase is associated with simian-virus-40 chromatin

1980

Otto, B.; Bohm, J.; Knippers, R.

Eur. J. Biochem.

112

363-366

487077

7130185

Studies on histone acetyltransferase. Partial purification and basic properties

1982

Wiktorowicz, J.E.; Bonner, J.

J. Biol. Chem.

257

12893-12900

487078

6783663

Histone acetylase from Drosophila melanogaster specific for H4

1981

Wiegand, R.C.; Brutlag, D.L.

J. Biol. Chem.

256

4578-4583

487079

7440548

Comparative studies of histone acetylation in nucleosomes, nuclei, and intact cells. Evidence for special factors which modify acetylase action

1980

Garcea, R.L.; Alberts, B.M.

J. Biol. Chem.

255

11454-11463

487080

7440547

Extensive purification of histone acetylase A, the major histone N-acetyl transferase activity detected in mammalian cell nuclei

1980

Belikoff, E.; Wong, L.J.; Alberts, B.M.

J. Biol. Chem.

255

11448-11453

487081

7356970

Histone-specific acetyltransferases from calf thymus. Isolation, properties, and substrate specificity of three different enzymes

1980

Sures, I.; Gallwitz, D.

Biochemistry

19

943-951

487082

6840090

Isolation and partial characterization of three histone-specific acetyltransferases from Artemia

1983

Estepa, I.; Pestana, A.

Eur. J. Biochem.

132

249-254

487083

7460927

Acetylation of nucleosomal histones in vitro

1980

Bohm, J.; Schlaeger, E.J.; Knippers, R.

Eur. J. Biochem.

112

353-362

487084

477673

Purification and properties of a histone acetyltransferase from Artemia salina, highly efficient with H1 histone

1979

Cano, A.; Pestana, A.

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