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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q5SQI0 | - |
- |
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 4345) and Asp46 are also involved | ? |
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 |