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Ligand [histone H2B]-L-lysine

Basic Ligand Information

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Roles as Enzyme Ligand

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

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.48

acetyl-CoA + [histone H2B]-L-lysine = CoA + [histone H2B]-N6-acetyl-L-lysine

756850

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Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Substrate (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.48

acetyl-CoA + [histone H2B]-L-lysine = CoA + [histone H2B]-N6-acetyl-L-lysine

756850

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2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine

734679, 734119

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2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine lysine

734117

-

2.3.2.24

2 entries

Product in Enzyme-catalyzed Reactions (3 results)

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Show Product (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.286

NAD+ + [histone H2B]-N6-acetyl-L-lysine12 = nicotinamide + [histone H2B]-L-lysine + 2'-O-acetyl-ADP-ribose

0

-

2.3.1.286

NAD+ + [histone H2B]-N6-myristoyl-L-lysine12 = nicotinamide + [histone H2B]-L-lysine + 2'-O-myristoyl-ADP-ribose

0

-

2.3.1.286

[histone H2B]-N6-acetyl-L-lysine + NAD+ + H2O = [histone H2B]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide

0

-

2.3.1.286

3 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.3.2.24

0.0022

-

E2 enzyme of 20 kDa, pH 7.5, 37°C

734119

2.3.2.24

0.0033

-

E2 enzyme of 32 kDa, pH 7.5, 37°C

734119

2.3.2.24

2 entries

K_M Value (2 results)

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Show KM Value (2 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.2.24

0.0015

-

E2 enzyme of 20 kDa, pH 7.5, 37°C

734119

2.3.2.24

0.012

-

E2 enzyme of 32 kDa, pH 7.5, 37°C

734119

2.3.2.24

2 entries

References & Links

Literature References (4)

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Show Reference (4 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

734117

2981864

Functional heterogeneity of ubiquitin carrier proteins

1985

Pickart, C.M.; Rose, I.A.

J. Biol. Chem.

260

1573-1581

734119

2843516

Functional diversity among putative E2 isozymes in the mechanism of ubiquitin-histone ligation

1988

Haas, A.L.; Bright, P.M.; Jackson, V.E.

J. Biol. Chem.

263

13268-13275

734679

7862115

Novel CDC34 (UBC3) ubiquitin-conjugating enzyme mutants obtained by charge-to-alanine scanning mutagenesis

1995

Pitluk, Z.W.; McDonough, M.; Sangan, P.; Gonda, D.K.

Mol. Cell. Biol.

15

1210-1219

756850

29676588

Lysine acetyltransferase inhibitors structure-activity relationships and potential therapeutic implications

2018

Fiorentino, F.; Mai, A.; Rotili, D.

Future Med. Chem.

10

1067-1091

Links to other databases for [histone H2B]-L-lysine

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