ExplorEnz: EC 2.3.1.108

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2.3.1.108

Accepted name:

α-tubulin N-acetyltransferase

Reaction:

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

Other name(s):

ATAT1 (gene name); MEC17 (gene name); α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase (ambiguous); acetyl-CoA:α-tubulin-L-lysine N-acetyltransferase; acetyl-CoA:[α-tubulin]-L-lysine 6-N-acetyltransferase

Systematic name:

acetyl-CoA:[α-tubulin]-L-lysine N⁶-acetyltransferase

Comments:

The enzyme is conserved from protists to mammals and is present in flowering plants. In most organisms it acetylates L-lysine at position 40 of α-tubulin.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99889-90-4

References:

1.	Greer, K., Maruta, H., L'Hernault, S.W. and Rosenbaum, J.L. α-Tubulin acetylase activity in isolated Chlamydomonas flagella. J. Cell Biol. 101 (1985) 2081–2084. [PMID: 4066751]
2.	Akella, J.S., Wloga, D., Kim, J., Starostina, N.G., Lyons-Abbott, S., Morrissette, N.S., Dougan, S.T., Kipreos, E.T. and Gaertig, J. MEC-17 is an α-tubulin acetyltransferase. Nature 467 (2010) 218–222. [DOI] [PMID: 20829795]
3.	Shida, T., Cueva, J.G., Xu, Z., Goodman, M.B. and Nachury, M.V. The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. USA 107 (2010) 21517–21522. [DOI] [PMID: 21068373]
4.	Taschner, M., Vetter, M. and Lorentzen, E. Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA. Proc. Natl. Acad. Sci. USA 109 (2012) 19649–19654. [DOI] [PMID: 23071318]
5.	Friedmann, D.R., Aguilar, A., Fan, J., Nachury, M.V. and Marmorstein, R. Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc. Natl. Acad. Sci. USA 109 (2012) 19655–19660. [DOI] [PMID: 23071314]
6.	Kalebic, N., Sorrentino, S., Perlas, E., Bolasco, G., Martinez, C. and Heppenstall, P.A. αTAT1 is the major α-tubulin acetyltransferase in mice. Nat. Commun. 4:1962 (2013). [DOI] [PMID: 23748901]

[EC 2.3.1.108 created 1989, modified 2021]