3.4.11.15: aminopeptidase Y
This is an abbreviated version!
For detailed information about aminopeptidase Y, go to the full flat file.
Word Map on EC 3.4.11.15
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3.4.11.15
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carboxypeptidase
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pyrococcus
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aminopeptidases
-
horikoshii
-
bestatin
-
p-nitroanilide
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griseus
-
lys-pna
- 3.4.11.15
- carboxypeptidase
-
pyrococcus
- aminopeptidases
- horikoshii
- bestatin
- p-nitroanilide
- griseus
-
lys-pna
Reaction
preferentially, release of N-terminal lysine =
Synonyms
AAP, aminopeptidase (cobalt-activated), aminopeptidase Co, APE3, LapB, lysine aminopeptidase, PF1861, PH1821, PhTET3, TET3, yylAPE
ECTree
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Metals Ions
Metals Ions on EC 3.4.11.15 - aminopeptidase Y
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Co2+
KCl
the enzyme is optimally active at salt concentration between 0.075 and 0.25 M KCl. More than 70% of the activity is maintained at 2 M KCl
Zinc
Co2+
0.2 mM, 4fold stimulation. When the sample is preincubated with 0.2 mM Co2+ ions and subjected to gel filtration, only 10% of the activity remains, while addition of Co2+ (0.2 mM) to the reaction mixture completely restores enzyme activity. Co2+ions could not be replaced with other divalent (Ca2+, Cd2+, Cu2+, Fe2+, Mg2+, Mn2+, Ni2+, or Zn2+) or monovalent cations (Na+or K+) when used at concentrations of up to 0.2 mM
Co2+
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25fold enhancement of hydrolysis of Arg-7-amido-4-methylcoumarin and Lys-7-amido-4-methylcoumarin. Hydrolysis of substrates longer than tripeptide or dipeptide-7-amido-4-methylcoumarin is inhibited
Co2+
-
for spectroscopic studies the enzyme containing magnetically and spectroscopically silent Zn(II) ion is substituted with Co(II)
Zinc
the purified enzyme contains two equivalent of zinc per monomer. When zinc is removed by EDTA treatment, the complex dissociates into dimeric species