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Literature summary 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

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.20 150000
-
 2 * 150000 Gallus gallus
3.4.11.20 300000
-
 low angle laser light scattering-HPLC Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.20 Gallus gallus
-
 hen
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.11.20 glycoprotein
-
 Gallus gallus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.11.20 egg yolk
-
 Gallus gallus
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.4.11.20 dimer 2 * 150000 Gallus gallus