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Literature summary for 2.3.1.108 extracted from

  • Yuzawa, S.; Kamakura, S.; Hayase, J.; Sumimoto, H.
    Structural basis of cofactor-mediated stabilization and substrate recognition of the alpha-tubulin acetyltransferase alphaTAT1 (2015), Biochem. J., 467, 103-113.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
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 Homo sapiens
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 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q5SQI0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + alpha-tubulin L-lysine
-
 Homo sapiens 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 ?

General Information

General Information Comment Organism
physiological function 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 Homo sapiens