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Literature summary 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 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.15 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
3.5.1.15 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

EC Number Metals/Ions Comment Organism Structure
3.5.1.15 Zn2+ Zn2+-dependent enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.15 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
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Organism

EC Number Organism UniProt Comment Textmining
3.5.1.15 Homo sapiens P45381
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.15 N-acetyl-L-aspartate + H2O
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 Homo sapiens acetate + L-aspartate
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 ?
3.5.1.15 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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 ?