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Enzyme Nomenclature
Information on EC 2.3.1.108 - alpha-tubulin N-acetyltransferase
Word Map on EC 2.3.1.108
- 2.3.1.108
- trna
-
anticodons
- histone
-
methionyl-trna
-
wobble
-
zymocin
-
formylation
-
aminoacylated
- dysautonomia
- aminoacyl-trnas
- rnapii
-
trnammet
-
met-trnafmet
-
transformylase
-
six-subunit
-
misacylated
-
ikbkap
- trnaphe
-
formyltransferase
-
p-site
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.3.1.108
-
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RECOMMENDED NAME
GeneOntology No.
alpha-tubulin N-acetyltransferase
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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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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:[alpha-tubulin]-L-lysine N6-acetyltransferase
The enzyme from Chlamydomonas flagella also acetylates mammalian brain alpha-tubulin.
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CAS REGISTRY NUMBER
COMMENTARY
99889-90-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
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a balance of acetylation and deaceylation by ATAT1/HDAC6, histone deacetylase 6, enzymes with opposite activities regulates the migratory and invasive capacities of breast tumor cells
physiological function
additional information
-
MEC-17 sequences are absent from Chlamydomonas reinhardtii, an organism that has alphaTAT activity
evolution
-
distribution of alphaTAT/MEC-17 across all eukaryotic clades reveals that it was present in the last eukaryotic common ancestor, which was ciliated
evolution
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distribution of alphaTAT/MEC-17 across all eukaryotic clades reveals that it was present in the last eukaryotic common ancestor, which was ciliated
evolution
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distribution of alphaTAT/MEC-17 across all eukaryotic clades reveals that it was present in the last eukaryotic common ancestor, which was ciliated
malfunction
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touch receptor neurons in mec-17 but not atat-2 mutants exhibit morphological defects, phenotype, overview. Both mec-17(ok2109) and mec-17(u265) produced an increase in the length of the touch receptor neuron processes, effects on touch receptor neuron microtubule organization and structure, overview. Enzymatically inactive MEC-17 mutants rescue some of the mec-17 phenotypes, the function of mec-17 is protein-dependent
malfunction
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overexpression of ATAT1 phenocopies the effect of HDAC6 inhibition by trichostatin. Random invasive migration of cells in 3D collagen I is inhibited by 40-50% upon MT1-MMP or ATAT1 knockdown
malfunction
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MEC-12 is the only alpha-tubulin with K40, and mec-12(e1607) probable null allele worms have greatly reduced touch responses. Intergration of single transgenes encoding MEC-12 with either wild-type K40 or K40R or K40Q substitutions into the mec-12(e1607)mutant using Mos1 transposon excision repair restores the levels of touch response to 80% of wild type level,whereas animals with either MEC-12-K40R or MEC-12-K40Q show reduced touch response, overview
malfunction
-
zebrafish embryos depleted in MEC-17 show a dramatic loss of acetyl-K40 in neurons but not in cilia. Depletion of MEC-17 in zebrafish, by injection with random sequence morpholinos or 5-bp mismatched morpholinos, produces phenotypes consistent with neuromuscular defects
malfunction
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disruption of the Tetrahymena MEC-17 gene, resulting in a marked loss of acetyl-K40 in Tetrahymena cells, phenocopies the K40R alpha-tubulin mutation and makes microtubules more labile. Overexpression of GFP-Mec17p in Tetrahymena greatly increases acetylation of microtubules
malfunction
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loss of Caenorhabditis elegans alphaTAT activity in the mec-17, atat-2 double mutant affects touch receptor neuron mechanosensation to a greater extent than having a nonacetylatable MEC-12 (K40R) form of tubulin in the organism
malfunction
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a delay in cilium formation for cultured human cells depleted of alphaTAT/MEC-17
malfunction
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disrupting MEC17 in Tetrahymena abolishes tubulin acetylation, but no overt defect in cilium formation or motility occurs
malfunction
-
in animals lacking MEC-17, alphaTAT-2, and the sole Caenorhabditis elegans K40 alpha-tubulin MEC-12, touch sensation can be restored by expression of an acetyl-mimic MEC-12 K40Q. Transient overexpression of alphaTAT1 in PtK2 cells is sufficient to acetylate nearly all microtubules, whereas catalytically inactive alphaTAT1 D157N or the HAT Elp3 fail to detectably elevate alpha-tubulin K40 acetylation
physiological function
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elongator, a GTPase component of the hyperphosphorylated holoenzyme RNA polymerase II, is a regulator of alpha-tubulin acetylation in vivo. Elongator is important for microtubule function in correct loading and velocity of vesicles in vivo, and acetylation has a function in fine-tuning intrinsic dynamics of microtubules by modulating alpha-tubulin turnover
physiological function
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the enzymatic activity of the alpha-tubulin acetyltransferase MEC-17 allows the production of 15-p microtubules in the touch receptor neurons microtubules, specific role for alpha-TAT in the formation of microtubules and in the production of higher order microtubules arrays. The alpha-TAT protein has functions that require acetyltransferase activity, such as the determination of protofilament number, and others that do not, e.g. presence of internal microtubule structures. Mec-17 and atat-2 are needed for touch sensitivity and MEC-12 acetylation
physiological function
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dynamics and distribution of MT1-MMP-positive endosomes require regulation of acetylation levels, ATAT1 tubulin acetyltransferase binds and regulates cortactin acetylation levels. Acetylation of alpha-tubulin mostly occurs on lysine residue 40, which is localized in the microtubule lumen. ATAT1 colocalizes with cortactin at the adherent surface of the cells and it is required for 2D migration and invasive migration of MDA-MB-231 cells in collagen matrix
physiological function
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MEC-17 is required for the function of touch receptor neurons in Caenorhabditis elegans and acts as a K40-specific acetyltransferase for alpha-tubulin. W06B11.1 os also required for acetylation of K40 and contribute to touch sensation
physiological function
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the K40 residue of alpha-tubulin is not required for survival in protists, such as Chlamydomonas
physiological function
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the K40 residue of alpha-tubulin is important in vertebrates, acetyl-K40-carrying microtubules are abundant in the nervous system, including the brain, optical nerves, spinal cord, and axons of peripheral nerves. MEC-17 is required for K40 acetylation in zebrafish and normal embryonic development
physiological function
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the K40 residue of alpha-tubulin is important in vertebrates, MEC-17 controls the levels of microtubule acetylation in mammalian cells
physiological function
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the K40 residue of alpha-tubulin is not required for survival in protists, such as Tetrahymena
physiological function
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MEC-17 and ATAT-2 are required for body touch sensation, which depends on the nonciliated, acetylated tubulin-containing touch receptor neurons. ATAT-2 is needed for acetylating tubulin in dendritic processes and cilia in those neurons. Additional role(s) for the acetyltransferase independent of tubulin acetylation
physiological function
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alphaTAT1 is the major and possibly the sole alpha-tubulin K40 acetyltransferase in mammals and nematodes, and tubulin acetylation plays a conserved role in several microtubule-based processes. The worm incorporates acetylated alpha-tubulin into their microtubules. alphaTAT1 is required for the acetylation of axonemal microtubules. In Caenorhabditis elegans, microtubule acetylation is most prominent in touch receptor neurons and MEC-17, a homologue of alphaTAT1, and its paralogue alphaTAT-2 are required for alpha-tubulin acetylation and for two distinct types of touch sensation. Worm mechanosensation requires K40 alpha-tubulin acetylation
physiological function
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acetylation of alpha-tubulin is up-regulated during adipogenesis, and adipocyte development is dependent on alpha-tubulin acetylation. Acetylation of alpha-tubulin is under the control of the acetyltransferase MEC-17 and deacetylases SIRT2 and HDAC6. Adipocyte development is inhibited in MEC-17-knockdown cells, but enhanced in MEC-17-overexpressing cells. Katanin, a microtubule-severing protein with enhanced activity on acetylated alpha-tubulin, is actively involved in adipogenesis
physiological function
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AcCoA and CoA each form a stable complex with human alphaTAT1 to maintain the protein integrity both in vivo and in vitro. The invariant residues Arg132 and Ser160 in alphaTAT1 participate in the stable interaction both with AcCoA and with CoA
physiological function
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loss of MEC-17 leads to microtubule instability, a reduction in mitochondrial number, and disrupted axonal transport, with altered distribution of both mitochondria and synaptic components. MEC-17-mediated axonal degeneration occurs independently from its acetyltransferase domain, it is enhanced by mutation of coel-1, a tubulin-associated molecule; and correlates with the animal’s body length
physiological function
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despite the confined intraluminal location of microtubule residue Lys40, TAT efficiently scans the microtubule bidirectionally and acetylates stochastically without preference for ends. TAT catalytic activity, not constrained luminal diffusion, is rate limiting for acetylation
physiological function
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alphaTAT1 promotes microtubule destabilization and accelerates microtubule dynamics. This effect persists in an alphaTAT1 mutant with no acetyltransferase activity, suggesting that interaction of alphaTAT1 with microtubules is the critical factor regulating microtubule stability
physiological function
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mice with a targeted deletion of Atat1 display a loss of detectable K40 alpha-tubulin acetylation across multiple tissues and in cellular structures such as cilia and axons where acetylation is normally enriched. Mice are viable and develop normally, however, the absence of Atat1 impacts upon sperm motility and male mouse fertility, and increases microtubule stability
physiological function
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macrophages challenged by bacterial lipopolysaccharides undergo extensive microtubule acetylation. Suppression of lipopolysaccharide-induced microtubule acetylation by inactivating the tubulin acetyltransferase, MEC17, profoundly inhibits the induction of anti-inflammatory interlukin-10, a phenotype effectively reversed by an acetylation-mimicking alpha-tubulin mutant. Reversible microtubule acetylation is a kinase signaling modulator and a key component in the inflammatory response
physiological function
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clathrin-coated pits control microtubule acetylation through a direct interaction of the alpha-tubulin acetyltransferase alphaTAT1 with the clathrin adaptor AP-2. About one-third of growing microtubule (+) ends contacts and pauses at clathrin-coated pits and loss of clathrin-coated pits decreased tubulin K40 acetylation levels. alphaTAT1 localises to clathrin-coated pits through a direct interaction with AP-2 that is required for microtubule acetylation. In migrating cells, the polarized orientation of acetylated microtubules correlates with clathrin-coated pits accumulation at the leading edge 10, and interaction of alphaTAT1 with AP-2 is required for directional migration
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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-tubulin L-lysine40
CoA + alpha-tubulin N6-acetyl-L-lysine40
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-
-
-
?
acetyl-CoA + [alpha-TAT1]-L-lysine
CoA + [alpha-TAT1]-N6-acetyl-L-lysine
-
-
enzyme TAT1 acetylates itself in a regulatory mechanism that is required for effective modification of tubulin. Acetylation of multiple lysine residues on itself
-
?
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
-
-
-
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
-
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
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin from calf is acetylated
-
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin from Chlamydomonas is acetylated
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
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alpha-tubulin from Chlamydomonas is acetylated
-
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
-
post-translational modification of alpha-tubulin
-
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
-
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
-
-
?
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
-
alpha-tubulin residue Ser38 is crucial for substrate recognition,whereas Asp39, Ile42, the glycine stretch (amino acid residues 43–45) and Asp46 are also involved
-
?
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-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
-
-
?
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
-
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
-
-
?
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
-
-
?
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
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-
-
additional information
?
-
-
wild-type adults have a strong signal for acetylated alpha-tubulin in the six touch receptor neurons
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-
-
additional information
?
-
-
in vitro, MEC-17 exclusively acetylates Lys40 of alpha-tubulin
-
-
-
additional information
?
-
-
alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones
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-
-
additional information
?
-
-
recombinant GST-MEC-17 directly acetylates purified tubulin from the MEC17-KO strain in vitro
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-
-
additional information
?
-
-
alphaTAT/MEC-17 is a lysine acetyltransferase for tubulin and not histones
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
-
post-translational modification of alpha-tubulin
-
-
?
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
-
-
?
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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
at 1 mM, almost complete inhibition; inhibition is due to the binding of calcium to the tubulin dimer rather than to the enzyme itself
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lipopolysaccharide
-
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
2.8
alpha-tubulin L-lysine
Homo sapiens
-
mutant K103A, pH 6.9, 22°C; mutant Q131A, pH 6.9, 22°C; mutant R69A, pH 6.9, 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
710
alpha-tubulin L-lysine
Homo sapiens
-
mutant N182A, pH 6.9, 22°C; truncation variant 1-193, pH 6.9, 22°C
98883
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
acetylation of alpha-tubulin is up-regulated during adipogenesis, and adipocyte development is dependent on alpha-tubulin acetylation
-
strongest expression in nervous systems of embryonic and adult mice
-
ATAT1 is distributed to the motile cilia of multiciliated cells of the trachea
additional information
-
MEC-12 is present in touch receptor neurons and other (ciliated) neurons. mec-17 expression is limited to touch receptor neurons, its paralogue atat-2 is also expressed in some ciliated neurons
-
peripheral, acetyl-K40 alpha-tubulin is enriched in cilia and axons of neurons
-
primary cilia, inner and outer segments of retinal photoreceptor cells
additional information
-
most Caenorhabditis elegans-ciliated sensory neurons lack detectable acetylated tubulin
additional information
-
robust alpha-tubulin K40 acetylation in the touch receptor neurons
additional information
-
ATAT1 colocalizes with cortactin at the adherent surface of the cells, association of ATAT1 and cortactin at invadopodia, subcellular localization study, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
Golgi aparatus of spermatocytes and spermatids of testis
-
acetylation of alpha-tubulin K40 by alphaTAT1 inside the microtubule lumen
-
2fold preference for polymerized versus soluble tubulin
-
enzyme acetylated both dimers and polymers of tubulin
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
-
enzyme catalyzes acetylation of multiple lysine residues on itself. Autoacetylation of alphaTAT1 increases its catalytic activity at microtubules
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cocrystal structures with bisubstrate analogs, consisting of a substrate peptide covalently linked to CoA through Lys40, to 1.35 A resolution. Substrate residue Lys40 is engaged in a suboptimal active site
-
crystal structure of the catalytic core of human MEC-17 in complex with its cofactor acetyl-CoA at 1.7 A resolution. The MEC-17 core adopts a canonical Gcn5-related N-acetyltransferase (GNAT) fold that is decorated with extensive surface loops. A large, evolutionarily conserved hydrophobic surface patch is critical for enzymatic activity
-
no significant changes are observed in the architecture of microtubules or the conformation of tubulin upon acetylation, based on protofilament distributions or microtubule helical lattice parameters. No clear differences in tubulin structure are detected between cryo-EM reconstructions of maximally deacetylated or acetylated microtubules. The effect of acetylation must be highly localized and affect interaction with proteins that bind directly to the lumen of the microtubule. alpha-TAT1 is able to interact with the outside of the microtubule, at least partly through the tubulin C-termini
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged Mec-17 from Escherichia coli strain BL21 by glutathione affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATAT1, DNA and amino acid sequence determination and analysis, stable functional expression of EGFP-ATAT1 and mutant ATAT1D157N in MDA-MB-231 cells and in HeLa cells
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genes alphaTAT/MEC-17, phylogenetic analysis
MEC-17 sequences are absent from Chlamydomonas reinhardtii, an organism that has alphaTAT activity
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
construction of a Mec-17 disruption mutant. The MEC-17-KO Tetrahymena cells have a normal growth rate, but theMEC-17-KOcells grow more slowly than wild type on medium with the microtubule depolymerizing compound oryzalin. Conversely, the MEC-17 KO cells grew faster than wild-type cells in medium with paclitaxel, a microtubule-stabilizing drug. This drug phenotype is consistent with an increase in dynamics of microtubules in MEC17-KO cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D157N
F105A
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complete loss of activity; mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
F183A
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complete loss of activity; mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
F186A
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mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
F190A
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mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
K162A
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mutation in the acetyl-CoA binding pocket, mild effect on enzymatic activity
K169A
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mutation in the acetyl-CoA binding pocket, mild effect on enzymatic activity
L104A
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complete loss of activity; mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
L164A
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mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
L173A
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mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
N73A
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mutation in highly conserved surface patches adjacent to the substrate-binding groove, discernable effect on catalytic activity
P178A
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mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
Q131A
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mutation in the acetyl-CoA binding pocket, mild effect on enzymatic activity
Q179A
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complete loss of activity; mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
R132A
S160A
S66A
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mutation in highly conserved surface patches adjacent to the substrate-binding groove, discernable effect on catalytic activity
V184A
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mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
additional information
D157N
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R132A
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mutation leads to a drastic misfolding of the isolated alphaTAT1 catalytic domain in the absence of CoA and AcCoA but not in the presence of excess amounts of either cofactor. Mutant is degraded much faster than the wild-type protein
R132A
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mutation in the acetyl-CoA binding pocket, mild effect on enzymatic activity
S160A
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mutation leads to a drastic misfolding of the isolated alphaTAT1 catalytic domain in the absence of CoA and AcCoA but not in the presence of excess amounts of either cofactor. Mutant is degraded much faster than the wild-type protein
S160A
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mutation in the acetyl-CoA binding pocket, mild effect on enzymatic activity
additional information
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in an mec-12(e1607) background, i.e. a putative null mutant, acetylation of microtubules is absent in all developmental stages
additional information
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overexpression of ATAT1 phenocopies the effect of HDAC6 inhibition by trichostatin
additional information
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expression of truncated variants, residues 1-193 and residues 1-236. Truncation mutant 1-193 exhibits a 3 times higher Km value than 1-236
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.108)
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