Literature summary for 3.5.1.15 extracted from

Kots, E.D.; Khrenova, M.G.; Nemukhin, A.V.
Allosteric control of N-acetyl-aspartate hydrolysis by the Y231C and F295S mutants of human aspartoacylase (2019), J. Chem. Inf. Model., 59, 2299-2308 .

Search for more literature for 3.5.1.15

Protein Variants

Protein Variants	Comment	Organism
F295S	the decreased availability of the active site for substrate molecules in the mutated enzymes explains their diminishing activity observed in clinical experiments. The variant is associated with the mild or variable form of Canavan disease	Homo sapiens
Y231C	the decreased availability of the active site for substrate molecules in the mutated enzymes explains their diminishing activity observed in clinical experiments. The variant is associated with the mild or variable form of Canavan disease	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	Zn2+-dependent enzyme	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	the enzyme hydrolyzes one of the most abundant amino acid derivatives in the brain, N-acetyl-aspartate	acetate + L-aspartate	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P45381	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-acetyl-L-aspartate + H2O	-	Homo sapiens	acetate + L-aspartate	-	?
N-acetyl-L-aspartate + H2O	the enzyme hydrolyzes one of the most abundant amino acid derivatives in the brain, N-acetyl-aspartate	Homo sapiens	acetate + L-aspartate	-	?

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Release 2023.1 (January 2023)