Information on EC 2.3.1.108 - alpha-tubulin N-acetyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.108
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RECOMMENDED NAME
GeneOntology No.
alpha-tubulin N-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N6-acetyl-L-lysine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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.
CAS REGISTRY NUMBER
COMMENTARY hide
99889-90-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
strain 21 gr, vegetative cells
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Potorous tridactylis Ptk-2 cells
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene MEC17
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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MEC-17 sequences are absent from Chlamydomonas reinhardtii, an organism that has alphaTAT activity
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
show the reaction diagram
acetyl-CoA + alpha-tubulin L-lysine40
CoA + alpha-tubulin N6-acetyl-L-lysine40
show the reaction diagram
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-
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?
acetyl-CoA + cortactin
CoA + N-acetyl-cortactin
show the reaction diagram
acetyl-CoA + [alpha-TAT1]-L-lysine
CoA + [alpha-TAT1]-N6-acetyl-L-lysine
show the reaction diagram
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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
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + alpha-tubulin L-lysine
CoA + alpha-tubulin N6-acetyl-L-lysine
show the reaction diagram
acetyl-CoA + cortactin
CoA + N-acetyl-cortactin
show the reaction diagram
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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
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
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competitive inhibitor
Colchicine
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at 0.001 mM is inhibitory to microtubule acetylation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lipopolysaccharide
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macrophages challenged by bacterial lipopolysaccharides undergo extensive microtubule acetylation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.003
acetyl-CoA
0.0035 - 0.1073
alpha-tubulin L-lysine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 9.2
alpha-tubulin L-lysine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
260 - 2780
alpha-tubulin L-lysine
98883
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
CoA
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competitive inhibitor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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acetylation of alpha-tubulin is up-regulated during adipogenesis, and adipocyte development is dependent on alpha-tubulin acetylation
Manually annotated by BRENDA team
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dorsal root ganglion
Manually annotated by BRENDA team
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primary cilia of the renal medullary collecting duct
Manually annotated by BRENDA team
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strongest expression in nervous systems of embryonic and adult mice
Manually annotated by BRENDA team
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ATAT1 is distributed to the motile cilia of multiciliated cells of the trachea
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Golgi aparatus of spermatocytes and spermatids of testis
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
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most prominent polypeptide, SDS-PAGE
130000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 67000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
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enzyme catalyzes acetylation of multiple lysine residues on itself. Autoacetylation of alphaTAT1 increases its catalytic activity at microtubules
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
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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
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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
partial
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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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expression of GST-tagged Mec-17 in Escherichia coli strain BL21
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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 hide
LITERATURE
D157N
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inactive mutant
C120A
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complete loss of activity
D157A
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complete loss of activity
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
I64A
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complete loss of activity
K102A
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complete loss of activity
K103A
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about 30% of wild-type 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
K98A
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complete loss of 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
L122A
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complete loss of 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
L60A
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complete loss of activity
N181A
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complete loss of activity
N182A
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about 25% of wild-type activity
N73A
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mutation in highly conserved surface patches adjacent to the substrate-binding groove, discernable effect on catalytic activity
P159A
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about 10% of wild-type 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
Q58A
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complete loss of activity
R158A
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about 45% of wild-type activity
R69A
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about 10% of wild-type activity
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
G134W/G136W/L139P
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loss of catalytic activity
additional information
Show AA Sequence (315 entries)
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