Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.11.7 extracted from

  • Tobe, H.; Kojima, F.; Aoyagi, T.; Umezawa, H.
    Purification by affinity chromatography using amastatin and properties of aminopeptidase A from pig kidney (1980), Biochim. Biophys. Acta, 613, 459-468.
    View publication on PubMed
Search for more literature for 3.4.11.7

Inhibitors

Inhibitors Comment Organism Structure
amastatin
-
 Sus scrofa
Cd2+
-
 Sus scrofa
Cu2+
-
 Sus scrofa
EDTA
-
 Sus scrofa
Hg2+
-
 Sus scrofa
Ni2+
-
 Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.091 1.2 Glu-beta-naphthylamide value depending on source of enzyme and presence of divalent cations Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ activation Sus scrofa
Ca2+ activation Sus scrofa
Sr2+ activation Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
300000
-
 gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
22.8
-
-
 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Glu-beta-naphthylamide + H2O
-
 Sus scrofa Glu + naphthylamine
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
 up to Sus scrofa
65
-
 up to in presence of CaCl2 Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Sus scrofa