2.3.1.108: alpha-tubulin N-acetyltransferase
This is an abbreviated version!
For detailed information about alpha-tubulin N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.108
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2.3.1.108
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trna
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histone
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chromatin
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anticodons
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wobble
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trnamet
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microtubule
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dysautonomia
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aminoacylated
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formylation
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cbp
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aminoacyl-trnas
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kluyveromyces
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zymocin
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methionyl-trna
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ikbkap
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trnaphe
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nua4
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rnapii
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six-subunit
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p-site
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non-histone
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complex-associated
- 2.3.1.108
- trna
- histone
- chromatin
-
anticodons
-
wobble
- trnamet
- microtubule
- dysautonomia
-
aminoacylated
-
formylation
- cbp
- aminoacyl-trnas
- kluyveromyces
-
zymocin
- methionyl-trna
-
ikbkap
- trnaphe
- nua4
- rnapii
-
six-subunit
-
p-site
-
non-histone
-
complex-associated
Reaction
Synonyms
acetyl-CoA:alpha-tubulin-L-lysine Ne-acetyltransferase, alpha-TAT, alpha-tubulin acetylase, alpha-tubulin acetyltransferase, alpha-tubulin K40 acetyltransferase, alpha-tubulin N-acetyltransferase 1, alphaTAT, alphaTAT1, alphaTAT2, ATAT-2, ATAT1, ATAT1 acetylase, ATAT1 tubulin acetyltransferase, elongator, KAT, lysine acetyltransferase, Mec-17, TAT, tubulin acetyltransferase
ECTree
2.3.1.108 alpha-tubulin N-acetyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.3.1.108 - alpha-tubulin N-acetyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D157N
F105A
F183A
F186A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
F190A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
K162A
mutation in the acetyl-CoA binding pocket, mild effect on enzymatic activity
K169A
mutation in the acetyl-CoA binding pocket, mild effect on enzymatic activity
L104A
L164A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
L173A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
N73A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, discernable effect on catalytic activity
P178A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
Q131A
mutation in the acetyl-CoA binding pocket, mild effect on enzymatic activity
Q179A
R132A
S160A
S66A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, discernable effect on catalytic activity
V184A
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
F105A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
F183A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
L104A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
Q179A
mutation in highly conserved surface patches adjacent to the substrate-binding groove, pronounced effetc on catalytic activity
R132A
mutation in the acetyl-CoA binding pocket, mild effect on enzymatic activity
R132A
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
mutation in the acetyl-CoA binding pocket, mild effect on enzymatic activity
S160A
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
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
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
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
