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Literature summary extracted from

  • Herga, S.; Brutus, A.; Vitale, R.M.; Miche, H.; Perrier, J.; Puigserver, A.; Scaloni, A.; Giardina, T.
    Site-directed mutagenesis and molecular modelling studies show the role of Asp82 and cysteines in rat acylase 1, a member of the M20 family (2005), Biochem. Biophys. Res. Commun., 330, 540-546.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.14 expression of GST-tagged wild-type and mutant enzymes in bacteria Rattus norvegicus

Protein Variants

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.14 Zn2+ metalloenzyme, required for activity Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.14 45000
-
 x * 45000, SDS-PAGE Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.14 Rattus norvegicus Q6AYS7 Wistar rats, gene ACY1
-

Purification (Commentary)

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

Reaction

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
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.14 kidney
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.1.14 additional information
-
-
 Rattus norvegicus

Substrates and Products (Substrate)

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
-
 ?

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.14 37
-
 assay at Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.14 8
-
 assay at Rattus norvegicus