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
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horikoshii
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bestatin
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p-nitroanilide
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griseus
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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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Subunits
Subunits on EC 3.4.11.15 - aminopeptidase Y
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dodecamer
monomer
tetramer
trimer
12 * 40000, SDS-PAGE, the active sites of the PhTET complexes are located inside the particles, in the catalytic chambers that are enclosed by the tetrahedron apices. The walls of these chambers are positively charged, and each one contains three active sites arranged in a circular way. Adjacent to the active sites, the specificity pockets appear as small cavities. The geometry of these pockets is different in each PhTET complex, as well as their location in the particles relative to the active sites. In PhTET3, the specificity pocket is formed by the side-chains of D262, T240, T295 and T297, which leads to a negative charge
dodecamer
studies on the parameters controlling the stability of the TET peptidase superstructure from Pyrococcus horikoshii reveal a crucial role of pH and catalytic metals in the oligomerization process. The dodecameric edifice of the enzyme remains intact under acidic pH. Basic pH leads to a significant deoligomerization. At pH 11 over 50% of the protein is still in its dodecameric form, revealing a great resistance of the edifice against deoligomerization. No unfolded or aggregated protein is found throughout the whole range of pH tested, indicating that the dimer is soluble and stable. Oligomerization is a metal dependent process