2.3.1.17: aspartate N-acetyltransferase
This is an abbreviated version!
For detailed information about aspartate N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.17
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2.3.1.17
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n-acetylaspartate
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canavan
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aspartoacylase
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n-acetyl-l-aspartate
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oligodendrocytes
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leukodystrophy
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8-like
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methamphetamine
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spongiform
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lipolysis
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n-acetylaspartylglutamate
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naags
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cholinergic
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medicine
- 2.3.1.17
- n-acetylaspartate
- canavan
- aspartoacylase
- n-acetyl-l-aspartate
- oligodendrocytes
- leukodystrophy
-
8-like
- methamphetamine
-
spongiform
-
lipolysis
- n-acetylaspartylglutamate
- naags
-
cholinergic
- medicine
Reaction
Synonyms
acetyltransferase, aspartate, ANAT, aspartate acetyltransferase, aspartate N-acetyltransferase, aspartic acetylase, L-aspartate N-acetyltransferase, NAT, NAT8L
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Inhibitors
Inhibitors on EC 2.3.1.17 - aspartate N-acetyltransferase
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glutamate
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Glutamate is a competitive inhibitor. No inhibition is observed with other amino acids, indicating that the enzyme is specific.
N-(2,6-dibromo-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
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N-(2,6-dichloro-4-carboxybenzyl)-N-carboxyethyl-3,4-dicarboxybenzylamine
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N-acetyl-(dimethyl)aspartyl-conjugated CoA
coenzyme A coupled to methylated N-acetyl aspartate, bisubstrate inhibitor
N-acetylaspartyl-conjugated CoA
coenzyme A coupled to N-acetyl aspartate, bisubstrate inhibitor
N-methyl-N-nonanoyl-beta-D-glucosylamine
Mega-9, high inhibition at CMC concentration
N-propionyl-(dimethyl)aspartyl-conjugated CoA
coenzyme A coupled to N-propionyl aspartate, bisubstrate inhibitor
N-[((2-[(tert-butoxycarbonyl)amino]ethyl)sulfanyl)acetyl]-L-aspartic acid
truncated bisubstrate analog
sodium 2-[(tert-butoxycarbonyl)amino]-3-[(2-([(1S)-1,2-dicarboxyethyl]amino)-2-oxoethyl)sulfanyl]propanoate
truncated bisubstrate analog
sodium 3-[(2-([(1S)-1,2-dicarboxyethyl]amino)-2-oxoethyl)sulfanyl]-2-([(trifluoromethoxy)carbonyl]amino)propanoate
truncated bisubstrate analog
effect of different detergents on the enzyme activity: non-ionic detergents such as Triton X-100 are less disruptive to protein structures than ionic detergents such as SDS, detergents such as C12E8, Tween 20 and several maltosides caused minimal disruption of the enzyme, with greater than 50% residual activity after incubation with CMC levels of each of these detergents. In contrast, significant loss of activity is observed upon incubation with C8 detergents, cymal5, octylglucoside and some shorter chain polymaleic anhydride (pmal) detergents. Ionic detergent SDS and a zwitterionic detergent lauryldimethylamine-N-oxide cause nearly complete loss of catalytic activity
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additional information
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effect of different detergents on the enzyme activity: non-ionic detergents such as Triton X-100 are less disruptive to protein structures than ionic detergents such as SDS, detergents such as C12E8, Tween 20 and several maltosides caused minimal disruption of the enzyme, with greater than 50% residual activity after incubation with CMC levels of each of these detergents. In contrast, significant loss of activity is observed upon incubation with C8 detergents, cymal5, octylglucoside and some shorter chain polymaleic anhydride (pmal) detergents. Ionic detergent SDS and a zwitterionic detergent lauryldimethylamine-N-oxide cause nearly complete loss of catalytic activity
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