2.3.1.17: aspartate N-acetyltransferase

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

Reaction

Synonyms

acetyltransferase, aspartate, ANAT, aspartate acetyltransferase, aspartate N-acetyltransferase, aspartic acetylase, L-aspartate N-acetyltransferase, NAT, NAT8L

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.17 aspartate N-acetyltransferase

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Results	in table
1	Activating Compound
16	AA Sequence
1	Application
1	CAS Registry Number
6	Cloned(Commentary)
3	Crystallization (Commentary)
45	Disease/ Diagnostics
2	General Information
2	IC50 Value
55	Inhibitors
24	Ki Value [mM]
30	KM Value [mM]
11	Localization
10	Metals/Ions
2	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
17	Organism
2	Pathway
3	pH Optimum
3	pH Range
15	Protein Variants
7	Purification (Commentary)
1	Reaction
1	Reaction Type
17	Reference
25	Source Tissue
6	Specific Activity [micromol/min/mg]
1	Storage Stability
24	Substrates and Products (Substrate)
4	Subunits
19	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Stability [°C]
5	Turnover Number [1/s]

General Information

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General Information on EC 2.3.1.17 - aspartate N-acetyltransferase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

Homo sapiens

Q8N9F0

Canavan disease is a fatal, neurological disease that is caused by an interruption in the metabolism of a critical amino acid, N-acetyl-L-aspartic acid. Defects at multiple locations in the aspA gene that codes for aspartoacylase, EC 3.5.1.15, lead to mutant forms of this enzyme that are either not expressed or rapidly degraded, or have significantly impaired catalytic activity, resulting in N-acetyl-L-aspartic acid accumulation. A second gene knock-out in the Nat8l gene which codes for aspartate N-acetyltransferase, the enzyme that synthesizes N-acetyl-L-aspartic acid, reverses these adverse effects, leading to normal myelination and a decrease in Canavan disease symptoms

737193

physiological function

Mus musculus

Q3UGX3

overexpression of Nat8L drains glucose-derived acetyl-CoA into the N-acetyl-L-aspartate pool at the expense of cellular lipids and certain amino acids. A combined activation of neutral and lysosomal (acid) lipolysis is responsible for the increased lipid degradation. Nat8l overexpression increases the number of autophagosomes and autolysosomes. Expression of Nat8l and aspartoacylase are nutritionally regulated and respond robustly to changes in glucose availability

756110