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Information on EC 2.3.1.108 - alpha-tubulin N-acetyltransferase
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EC Tree
2.3.1.108 alpha-tubulin N-acetyltransferaseIUBMB 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 alpha-tubulin.
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Word Map
- 2.3.1.108
- trna
- histone
- chromatin
-
anticodons
-
wobble
- trnamet
- microtubule
- dysautonomia
-
aminoacylated
-
formylation
- cbp
- aminoacyl-trnas
- kluyveromyces
-
zymocin
- methionyl-trna
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ikbkap
- trnaphe
- nua4
- rnapii
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six-subunit
-
p-site
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non-histone
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complex-associated
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
elongator, lysine acetyltransferase, atat1, mec-17, tubulin acetyltransferase, alpha-tubulin acetyltransferase, atat-2, alpha-tubulin n-acetyltransferase 1, atat1 tubulin acetyltransferase, alpha-tubulin n-acetyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl-CoA:alpha-tubulin-L-lysine Ne-acetyltransferase
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-
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alpha-TAT
alpha-tubulin acetylase
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-
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alpha-tubulin acetyltransferase
alpha-tubulin N-acetyltransferase 1
alphaTAT
alphaTAT1
ATAT1
Mec-17
alpha-tubulin acetyltransferase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
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-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:[alpha-tubulin]-L-lysine N6-acetyltransferase
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 alpha-tubulin.
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CAS REGISTRY NUMBER
COMMENTARY
99889-90-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + [alpha-TAT1]-L-lysine
CoA + [alpha-TAT1]-N6-acetyl-L-lysine
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enzyme TAT1 acetylates itself in a regulatory mechanism that is required for effective modification of tubulin. Acetylation of multiple lysine residues on itself
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?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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-
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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-
-
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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acetylation of the lysine residue at position 40
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?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin from calf is acetylated
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?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin from mouse is acetylated
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?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin from calf is acetylated
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-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin from Chlamydomonas is acetylated
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?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin from Chlamydomonas is acetylated
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-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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post-translational modification of alpha-tubulin
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-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin from calf is acetylated
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-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin from Chlamydomonas is acetylated
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-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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-
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin residue Ser38 is crucial for substrate recognition,whereas Asp39, Ile42, the glycine stretch (amino acid residues 4345) and Asp46 are also involved
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?
acetyl-CoA + cortactin
CoA + N-acetyl-cortactin
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ATAT1 acetylates, binds and colocalizes with cortactin at the adherent surface of MDA-MB-231 cells
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-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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-
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?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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acetylation of the epsilon-amino group of Lys40
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-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
K40 of alpha-tubulin is the sole site of acetylation by alphaTAT1, alphaTAT1 specifically acetylates K40 of alpha-tubulin and prefers microtubules over free tubulin, overview
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?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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alphaTAT1 acetylates tubulin through its GNAT domain in vitro. K40 of alpha-tubulin is the sole site of acetylation by alphaTAT1. alphaTAT1 displays a greater catalytic efficiency for taxol-stabilized microtubules than for free tubulin
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?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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acetylation of the epsilon-amino group of Lys40
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-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
acetylation of the epsilon-amino group of Lys40
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-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
acetylation of alpha-tubulin mostly occurs on lysine residue 40, which is localized in the microtubule lumen
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?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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acetylation of the epsilon-amino group of Lys40
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-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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-
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-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
acetylation of the epsilon-amino group of Lys40
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-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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acetylation of the epsilon-amino group of Lys40, in Tetrahymena, alpha-tubulin is the major if not the only substrate of MEC-17-dependent K acetylation
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?
acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
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?
acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
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?
acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
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?
additional information
?
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alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones
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?
additional information
?
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wild-type adults have a strong signal for acetylated alpha-tubulin in the six touch receptor neurons
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?
additional information
?
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in vitro, MEC-17 exclusively acetylates Lys40 of alpha-tubulin
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?
additional information
?
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alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones
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?
additional information
?
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the enzyme shows tubulin-specific acetylation activity
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additional information
?
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the enzyme shows tubulin-specific acetylation activity
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additional information
?
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recombinant GST-MEC-17 directly acetylates purified tubulin from the MEC17-KO strain in vitro
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?
additional information
?
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alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + cortactin
CoA + N-acetyl-cortactin
-
ATAT1 acetylates, binds and colocalizes with cortactin at the adherent surface of MDA-MB-231 cells
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
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-
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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-
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?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
-
post-translational modification of alpha-tubulin
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-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
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-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
acetylation of the epsilon-amino group of Lys40
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-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
K40 of alpha-tubulin is the sole site of acetylation by alphaTAT1, alphaTAT1 specifically acetylates K40 of alpha-tubulin and prefers microtubules over free tubulin, overview
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
acetylation of the epsilon-amino group of Lys40
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
acetylation of the epsilon-amino group of Lys40
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
acetylation of alpha-tubulin mostly occurs on lysine residue 40, which is localized in the microtubule lumen
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
acetylation of the epsilon-amino group of Lys40
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
acetylation of the epsilon-amino group of Lys40, in Tetrahymena, alpha-tubulin is the major if not the only substrate of MEC-17-dependent K acetylation
-
-
?
additional information
?
-
-
alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones
-
-
?
additional information
?
-
-
wild-type adults have a strong signal for acetylated alpha-tubulin in the six touch receptor neurons
-
-
?
additional information
?
-
-
alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones
-
-
?
additional information
?
-
-
alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
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at 1 mM, almost complete inhibition; inhibition is due to the binding of calcium to the tubulin dimer rather than to the enzyme itself
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
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additional information
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analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lipopolysaccharide
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macrophages challenged by bacterial lipopolysaccharides undergo extensive microtubule acetylation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
560