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Literature summary for 3.4.11.14 extracted from

  • Garner, C.W.; Behal, F.J.
    Human liver aminopeptidase. Role of metal ions in mechanism of action (1974), Biochemistry, 13, 3227-3233.
    View publication on PubMed
Search for more literature for 3.4.11.14

General Stability

General Stability Organism
when the enzyme is treated at 60°C with EDTA the inhibition is no longer reversible and there is a concomitant loss of zinc Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline 99% inhibition at 0.5 mM; Ki 0.028 mM Homo sapiens
2,2'-bipyridine 5.0 mM, 29% inhibition Homo sapiens
2,9-Dimethyl-1,10-phenanthroline 2.0 mM, 52% inhibition Homo sapiens
8-hydroxyquinoline 2.0 mM, 84% inhibition Homo sapiens
azide 92% inhibition at 10 mM Homo sapiens
cyanide 84% inhibition at 10 mM Homo sapiens
EDTA 98% inhibition at 0.001 mM Homo sapiens
EGTA 96% inhibition at 1 mM; Ki 0.012 mM Homo sapiens
KCN 10 mM, 84% inhibition Homo sapiens
Na2S 10 mM, 92% inhibition Homo sapiens
oxalate 50 mM ammonium oxalate, 71% inhibition Homo sapiens
Sulfide
-
 Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ Km: 0.05 mM Homo sapiens
Co2+ 2.4fold activation, Co2+ binds loosely in a noncompetitive manner Homo sapiens
Zinc 8.3 nanoatoms of tightly bound zinc per mg of protein Homo sapiens
Zinc zinc is located near the substrate binding site Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
-

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.012
-
 EGTA
-
 Homo sapiens
0.028
-
 1,10-phenanthroline
-
 Homo sapiens
0.076
-
 Sulfide
-
 Homo sapiens