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Literature summary extracted from

  • Le Coq, J.; Pavlovsky, A.; Malik, R.; Sanishvili, R.; Xu, C.; Viola, R.E.
    Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue (2008), Biochemistry, 47, 3484-3492.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.15 expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.15 crystallization in complex with inhibitor N-phosphonomethyl-L-aspartate, crystallization conditions: 50 mM sodium citrate (pH 6.0), 300 mM K2HPO4, and 15-19% polyethylene glycol 3350 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.15 E178D 10% activity of native enzyme Homo sapiens
3.5.1.15 E24A no detectable activity Homo sapiens
3.5.1.15 E24D no detectable activity Homo sapiens
3.5.1.15 E24G no protein expression Homo sapiens
3.5.1.15 H116A no detectable activity Homo sapiens
3.5.1.15 H21A no detectable activity Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.15 N-phosphonomethyl-L-aspartate
-
 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.15 Zn2+ one zinc ion per monomer 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 malfunction of the enzyme causes Canavan disease L-aspartate + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.15 Homo sapiens P45381
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.15 anion exchange chromatography followed by size exclusion chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.15 brain
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.15 N-acetyl-L-aspartate + H2O malfunction of the enzyme causes Canavan disease Homo sapiens L-aspartate + acetate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.15 homodimer extensive contact surface area between the two subunits Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.5.1.15 Aspartoacylase
-
 Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.5.1.15 0.3
-
 N-phosphonomethyl-L-aspartate
-
 Homo sapiens