EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.1.15 | A305E | 10% activity compared to native enzyme form, mutation responsible for the Canavan disease | Homo sapiens |
3.5.1.15 | C152R | 0.5% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease | Homo sapiens |
3.5.1.15 | C152W | 1% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease | Homo sapiens |
3.5.1.15 | E285A | 0.3% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease | Homo sapiens |
3.5.1.15 | E285A/P181T | 32% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease | Homo sapiens |
3.5.1.15 | F295S | 10% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease | Homo sapiens |
3.5.1.15 | R71H | 11% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease | Homo sapiens |
3.5.1.15 | Y231C | 24% activity compared to native enzyme form, the stabilities against denaturation induced by heating and by a 1 M urea solution (conformational stability) are considerably lower for the mutant than for native form of the enzyme, mutation responsible for the Canavan disease | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.15 | N-acetyl-L-aspartate | substrate inhibition at high concentration | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.15 | 0.21 | - |
N-trifluoroacetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 0.23 | - |
N-dichloroacetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 0.36 | - |
N-acetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 0.59 | - |
N-Chloroacetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 0.95 | - |
N-formyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.15 | Zn2+ | zinc-dependent enzyme. Zn2+ coordination region: His21, Glu24 and His116 | Homo sapiens |
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 | aspartoacylase is a key enzyme in the human central nervous system. N-Acetyl-L-aspartate is a precursor for the synthesis of the dipeptide N-acetylaspartyl-glutamate, which participates in the neuromodulation of metabotropic and NMDA receptors (NMDA is N-methyl-D-aspartate), regulates the intracellular pressure in neurons and is involved in the energy generation from glutamate anions in neuronal mitochondria. N-Acetyl-L-aspartate is a source of acetyl groups for the construction of myelin sheath in the brain. Therefore, maintenance of the N-acetyl-L-aspartate level ensures proper development and functions of white matter | acetate + L-aspartate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.15 | Homo sapiens | P45381 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.15 | N-acetyl-L-aspartate + H2O | - |
Homo sapiens | acetate + L-aspartate | - |
? | |
3.5.1.15 | N-acetyl-L-aspartate + H2O | aspartoacylase is a key enzyme in the human central nervous system. N-Acetyl-L-aspartate is a precursor for the synthesis of the dipeptide N-acetylaspartyl-glutamate, which participates in the neuromodulation of metabotropic and NMDA receptors (NMDA is N-methyl-D-aspartate), regulates the intracellular pressure in neurons and is involved in the energy generation from glutamate anions in neuronal mitochondria. N-Acetyl-L-aspartate is a source of acetyl groups for the construction of myelin sheath in the brain. Therefore, maintenance of the N-acetyl-L-aspartate level ensures proper development and functions of white matter | Homo sapiens | acetate + L-aspartate | - |
? | |
3.5.1.15 | N-chloroacetyl-L-aspartate + H2O | - |
Homo sapiens | chloroacetate + L-aspartate | - |
? | |
3.5.1.15 | N-dichloroacetyl-L-aspartate + H2O | - |
Homo sapiens | dichloroacetate + L-aspartate | - |
? | |
3.5.1.15 | N-formyl-L-aspartate + H2O | - |
Homo sapiens | formate + L-aspartate | - |
? | |
3.5.1.15 | N-trifluoroacetyl-L-aspartate + H2O | - |
Homo sapiens | trifluoroacetate + L-aspartate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.1.15 | homodimer | - |
Homo sapiens |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.15 | 0.083 | - |
N-acetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 0.25 | - |
N-formyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 0.62 | - |
N-Chloroacetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 0.77 | - |
N-dichloroacetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 1.2 | - |
N-trifluoroacetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.1.15 | malfunction | catalytic deficiency of aspartoacylase is associated with several neurodegenerative disorders. The Canavan disease occurs most frequently in Ashkenazi Jews, with more than 96% of cases being associated with two point mutations: Glu285Ala and Tyr231X. The Canavan disease in other ethnic groups is associated with a more diverse range of mutations, the Ala305Glu replacement being the most frequent | Homo sapiens |
3.5.1.15 | physiological function | aspartoacylase is a key enzyme in the human central nervous system | Homo sapiens |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.15 | 0.23 | - |
N-acetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 0.26 | - |
N-formyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 1 | - |
N-Chloroacetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 3.4 | - |
N-dichloroacetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens | |
3.5.1.15 | 5.8 | - |
N-trifluoroacetyl-L-aspartate | pH and temperature not specified in the publication | Homo sapiens |