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
67000
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2 * 67000, 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 (438 entries)
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