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Literature summary for 3.4.11.20 extracted from

  • Tanaka, T.; Ichishima, E.
    Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme (1993), Int. J. Biochem., 25, 1681-1688.
    View publication on PubMed
Search for more literature for 3.4.11.20

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates the inactive, Zn2+-free apoenzyme Gallus gallus
Cd2+ activates the inactive, Zn2+-free apoenzyme Gallus gallus
Co2+ activates the inactive, Zn2+-free apoenzyme Gallus gallus
Cu2+ activates the inactive, Zn2+-free apoenzyme Gallus gallus
Mn2+ activates the inactive, Zn2+-free apoenzyme Gallus gallus
additional information no activation of the inactive, Zn2+-free apoenzyme by Mg2+ and Fe2+ Gallus gallus
Ni2+ activates the inactive, Zn2+-free apoenzyme Gallus gallus
Zinc activates the inactive, Zn2+-free apoenzyme Gallus gallus
Zinc a zinc protein, contains 1.0 gatom of zinc/mol of a subunit Gallus gallus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
 2 * 150000 Gallus gallus
300000
-
 low angle laser light scattering-HPLC Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
 hen
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
egg yolk
-
 Gallus gallus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Leu 4-nitroanilide + H2O
-
 Gallus gallus ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 150000 Gallus gallus