Literature summary for 3.5.1.14 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.

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Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
C23A	site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme	Rattus norvegicus
C272A	site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme	Rattus norvegicus
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
C331A	site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme	Rattus norvegicus
C49A	site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme	Rattus norvegicus
D82E	site-directed mutagenesis, the mutant shows highly reduced activity and loss of zinc coordination compared to the wild-type enzyme	Rattus norvegicus
D82N	site-directed mutagenesis, nearly inactive mutant	Rattus norvegicus

Metals/Ions

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

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
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

Reaction	Comment	Organism	Reaction ID
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

Source Tissue	Comment	Organism	Textmining
kidney	-	Rattus norvegicus	-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-acetyl-L-leucine + H2O	-	Rattus norvegicus	acetate + L-leucine	-	?
N-acetyl-L-methionine + H2O	-	Rattus norvegicus	acetate + L-methionine	-	?

Subunits

Subunits	Comment	Organism
?	x * 45000, SDS-PAGE	Rattus norvegicus
More	structure molecular modelling	Rattus norvegicus

Synonyms

Synonyms	Comment	Organism
ACY-1A	-	Rattus norvegicus
acylase 1	-	Rattus norvegicus
aminoacylase 1a	-	Rattus norvegicus
More	the enzyme is a member of the metalloprotein family M20	Rattus norvegicus
N-acyl-L-amino-acid amidohydrolase	-	Rattus norvegicus

Temperature Optimum [°C]

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

pH Optimum

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

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Release 2023.1 (January 2023)