• BRENDA home

• Basic Ligand Information
• • Molecular Structure
  • Sum Formula
  • BRENDA Name
  • Synonyms
  • InChIKey
  • Pathways
• Roles as Enzyme Ligand
• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
• References & Links
• • References
  • Links

print visible entries

print all entries

Ligand [alpha-tubulin]-N6-acetyl-L-lysine

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

top print hide

Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.286

NAD+ + [alpha-tubulin]-N6-acyl-L-lysine = nicotinamide + [alpha-tubulin]-L-lysine + 2'-O-acyl-ADP-ribose

738674

-

3.5.1.98

N-acetyl-lysine-alpha-tubulin + H2O = acetate + alpha-tubulin

713487

-

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

top print hide

Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.108

acetyl-CoA + alpha-tubulin L-lysine = CoA + alpha-tubulin N6-acetyl-L-lysine

-

-

2.3.1.108

acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N6-acetyl-L-lysine

-

-

2.3.1.108

acetyl-CoA + [alpha-tubulin]-L-lysine40 = CoA + [alpha-tubulin]-N6-acetyl-L-lysine40

-

-

2.3.1.48

acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N6-acetyl-L-lysine

-

-

2.3.1.48

acetyl-CoA + [alpha-tubulin]-L-lysine40 = CoA + [alpha-tubulin]-N6-acetyl-L-lysine40

-

-

2.3.1.108

3 entries

2.3.1.48

2 entries

Substrate in Enzyme-catalyzed Reactions (6 results)

top print hide

Show Substrate (6 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.286

NAD+ + [alpha-tubulin peptide]-N6-acetyl-L-lysine = nicotinamide + [alpha-tubulin peptide]-L-lysine + 2'-O-acetyl-ADP-ribose

729603

-

2.3.1.286

NAD+ + [alpha-tubulin]-N6-acetyl-L-lysine40 = nicotinamide + [alpha-tubulin]-L-lysine40 + 2'-O-acetyl-ADP ribose

729674

-

2.3.1.286

[alpha-tubulin]-N6-acetyl-L-lysine40 + NAD+ + H2O = [alpha-tubulin]-L-lysine40 + 2''-O-acetyl-ADP-D-ribose + nicotinamide

750703

-

2.3.1.286

NAD+ + [alpha-tubulin]-N6-acyl-L-lysine = nicotinamide + [alpha-tubulin]-L-lysine + 2'-O-acyl-ADP-ribose

738674

-

3.5.1.98

acetyl-tubulin + H2O = tubulin + acetate

711850

-

3.5.1.98

N-acetyl-lysine-alpha-tubulin + H2O = acetate + alpha-tubulin

713487

-

2.3.1.286

4 entries

3.5.1.98

2 entries

Product in Enzyme-catalyzed Reactions (5 results)

top print hide

Show Product (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.108

acetyl-CoA + alpha-tubulin L-lysine = CoA + alpha-tubulin N6-acetyl-L-lysine

, 486115, 486116

-

2.3.1.108

acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N6-acetyl-L-lysine

-

-

2.3.1.108

acetyl-CoA + [alpha-tubulin]-L-lysine40 = CoA + [alpha-tubulin]-N6-acetyl-L-lysine40

-

-

2.3.1.48

acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N6-acetyl-L-lysine

-

-

2.3.1.48

acetyl-CoA + [alpha-tubulin]-L-lysine40 = CoA + [alpha-tubulin]-N6-acetyl-L-lysine40

-

-

2.3.1.108

3 entries

2.3.1.48

2 entries

Enzyme Kinetic Parameters

References & Links

Literature References (8)

top print hide

Show Reference (8 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

486115

9118990

Tubulin post-translational modifications

1997

MacRae, T.H.

Eur. J. Biochem.

244

265-278

486116

8135364

Assay of tubulin acetyltransferase activity in subcellular tissue fractions

1994

Lloyd, R.A.; Gentleman, S.; Chader, G.J.

Anal. Biochem.

216

42-46

711850

19910924

Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6

2010

Fiesel, F.C.; Voigt, A.; Weber, S.S.; Van den Haute, C.; Waldenmaier, A.; Goerner, K.; Walter, M.; Anderson, M.L.; Kern, J.V.; Rasse, T.M.; Schmidt, T.; Springer, W.; Kirchner, R.; Bonin, M.; Neumann, M.; Baekelandt, V.; Alunni-Fabbroni, M.; Schulz, J.B.; Kahle, P.J.

EMBO J.

29

209-221

713487

19329208

Epigenetic modulation of radiation response in human cancer cells with activated EGFR or HER-2 signaling: potential role of histone deacetylase 6

2009

Kim, I.A.; No, M.; Lee, J.M.; Shin, J.H.; Oh, J.S.; Choi, E.J.; Kim, I.H.; Atadja, P.; Bernhard, E.J.

Radiother. Oncol.

92

125-132

729603

25395356

The discovery of a highly selective 5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4(3H)-one SIRT2 inhibitor that is neuroprotective in an in vitro Parkinson's disease model

2015

Di Fruscia, P.; Zacharioudakis, E.; Liu, C.; Moniot, S.; Laohasinnarong, S.; Khongkow, M.; Harrison, I.F.; Koltsida, K.; Reynolds, C.R.; Schmidtkunz, K.; Jung, M.; Chapman, K.L.; Steegborn, C.; Dexter, D.T.; Sternberg, M.J.; Lam, E.W.; Fuchter, M.J.

ChemMedChem

10

69-82

729674

24602787

Development and characterization of 3-(benzylsulfonamido)benzamides as potent and selective SIRT2 inhibitors

2014

Khanfar, M.A.; Quinti, L.; Wang, H.; Choi, S.H.; Kazantsev, A.G.; Silverman, R.B.

Eur. J. Med. Chem.

76

414-426

738674

25666612

Propofol inhibits SIRT2 deacetylase through a conformation-specific, allosteric site

2015

Weiser, B.P.; Eckenhoff, R.G.

J. Biol. Chem.

290

8559-8568

750703

15128440

Sirtuins Sir2-related NAD-dependent protein deacetylases

2004

North, B.J.; Verdin, E.

Genome Biol.

5

224

Links to other databases for [alpha-tubulin]-N6-acetyl-L-lysine

top print hide

Show Links (1 entry)

ChEBI

PubChem

-