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Literature summary for 3.5.1.14 extracted from

  • Durand, A.; Giardina, T.; Villard, C.; Roussel, A.; Puigserver, A.; Perrier, J.
    Rat kidney acylase I: further characterization and mutation studies on the involvement of Glu 147 in the catalytic process (2003), Biochimie, 85, 953-962.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain BL21(DE3) Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
E147A completely inactive Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
gel filtration Rattus norvegicus
45847
-
3 * 45847, deduced from deduced aminacid sequence Rattus norvegicus
125000
-
gel filtration Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
rat
-

Purification (Commentary)

Purification (Comment) Organism
by a method that includes DEAE-Sepharose column, Chelating-Sepharose column, Amicon PM 30 membrane and Sephacryl-S200 column Rattus norvegicus

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
1.4
-
-
Rattus norvegicus
8.33
-
pH 8.0, 37°C Rattus norvegicus

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
monomer 1 * 44000, denaturing and reducing gels Rattus norvegicus
trimer 3 * 44000, gel filtration and SDS-PAGE Rattus norvegicus
trimer 3 * 45847, deduced from deduced aminacid sequence Rattus norvegicus