Literature summary for 3.5.1.15 extracted from

Kots, E.D.; Lushchekina, S.V.; Varfolomeev, S.D.; Nemukhin, A.V.
Role of protein dimeric interface in allosteric inhibition of N-acetyl-aspartate hydrolysis by human aspartoacylase (2017), J. Chem. Inf. Model., 57, 1999-2008 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
N-acetyl-aspartate	decrease of the reaction rate at high substrate concentrations. Binding of N-acetyl-aspartate to the allosteric site induces significant rigidity to the protein loops with the amino acid side chains forming gates to the enzyme active site	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
N-acetyl-L-aspartate + H2O	Homo sapiens	-	acetate + L-aspartate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P45381	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-acetyl-L-aspartate + H2O	-	Homo sapiens	acetate + L-aspartate	-	?

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Release 2023.1 (January 2023)