2.3.1.108: alpha-tubulin N-acetyltransferase

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For detailed information about alpha-tubulin N-acetyltransferase, go to the full flat file.

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 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.108 alpha-tubulin N-acetyltransferase

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Results	in table
1	Activating Compound
1631	AA Sequence
1	CAS Registry Number
9	Cloned(Commentary)
11	Cofactor
3	Crystallization (Commentary)
303	Disease/ Diagnostics
1	Expression
47	General Information
5	Inhibitors
20	kcat/KM [mM/s]
1	Ki Value [mM]
22	KM Value [mM]
22	Localization
6	Molecular Weight [Da]
20	Natural Substrates/ Products (Substrates)
40	Organism
18	PDB ID
5	pH Optimum
2	Posttranslational Modification
44	Protein Variants
3	Purification (Commentary)
1	Reaction
1	Reaction Type
39	Reference
36	Source Tissue
42	Substrates and Products (Substrate)
3	Subunits
53	Synonyms
1	Systematic Name
20	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.3.1.108 - alpha-tubulin N-acetyltransferase

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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

Homo sapiens

Q5SQI0

735916

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

Homo sapiens

Q5SQI0

736637

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

Homo sapiens

Q5SQI0

736778