EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.14 | expression of GST-tagged wild-type and mutant enzymes in bacteria | Rattus norvegicus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.1.14 | C23A | site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme | Rattus norvegicus |
3.5.1.14 | C272A | site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme | Rattus norvegicus |
3.5.1.14 | C294A | site-directed mutagenesis, the mutation causes a conformational change of the 3D-structure, the mutant shows highly reduced activity compared to the wild-type enzyme | Rattus norvegicus |
3.5.1.14 | C331A | site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme | Rattus norvegicus |
3.5.1.14 | C49A | site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme | Rattus norvegicus |
3.5.1.14 | D82E | site-directed mutagenesis, the mutant shows highly reduced activity and loss of zinc coordination compared to the wild-type enzyme | Rattus norvegicus |
3.5.1.14 | D82N | site-directed mutagenesis, nearly inactive mutant | Rattus norvegicus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.14 | Zn2+ | metalloenzyme, required for activity | Rattus norvegicus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.5.1.14 | 45000 | - |
x * 45000, SDS-PAGE | Rattus norvegicus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.14 | Rattus norvegicus | Q6AYS7 | Wistar rats, gene ACY1 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.1.14 | recombinant GST-tagged wild-type and mutant enzymes from bacteria by solubilization with Triton X-100 and 10% sarcosyl, glutathione affinity chromatography, and tag removal by thrombin | Rattus norvegicus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.5.1.14 | an N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate | active site structure, molecular modelling to determine Asp82 function in catalysis, Asp82 ensures a proper protonation of the catalytic His residue, overview | Rattus norvegicus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.5.1.14 | kidney | - |
Rattus norvegicus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.5.1.14 | additional information | - |
- |
Rattus norvegicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.14 | N-acetyl-L-leucine + H2O | - |
Rattus norvegicus | acetate + L-leucine | - |
? | |
3.5.1.14 | N-acetyl-L-methionine + H2O | - |
Rattus norvegicus | acetate + L-methionine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.1.14 | ? | x * 45000, SDS-PAGE | Rattus norvegicus |
3.5.1.14 | More | structure molecular modelling | Rattus norvegicus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.14 | ACY-1A | - |
Rattus norvegicus |
3.5.1.14 | acylase 1 | - |
Rattus norvegicus |
3.5.1.14 | aminoacylase 1a | - |
Rattus norvegicus |
3.5.1.14 | More | the enzyme is a member of the metalloprotein family M20 | Rattus norvegicus |
3.5.1.14 | N-acyl-L-amino-acid amidohydrolase | - |
Rattus norvegicus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.14 | 37 | - |
assay at | Rattus norvegicus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.14 | 8 | - |
assay at | Rattus norvegicus |