no activity with Gly-Pro-beta-naphthylamide, Z-Gly-Pro-beta-naphthylamide, Z-Gly-Ala-Pro-beta-naphthylamide, Z-Ala-Gly-Pro-beta-naphthylamide, Gly-Ala-Gly-Pro-beta-naphthylamide, Z-Gly-Ala-Gly-Pro-beta-naphthylamide, and Ala-Gly-Ala-Gly-Pro-beta-naphthylamide
activates, half-maximal activity at 650 nM. The enzyme is likely to be a Zn2+-dependent metalloenzyme, N-terminal region stabilizes Zn2+-binding. Atomic absorption spectroscopy reveals 0.26 atoms of Zn2+ per molecule. When the enzyme is denatured with 6 M guanidine hydrochloride and refolded in the presence of 4 mM Zn2+, it contains 0.53 atoms of Zn2+ per molecule with 1.5fold increase in activity
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Changes in spatio-temporal localization of tripeptidyl peptidase II (TPPII) in murine colon adenocarcinoma cells during aggresome formation: a microscopy study based on a novel fluorescent proteasome inhibitor.
hanging-drop vapour diffusion method at 20Â°C. Crystallization of aminotripeptidase and a derivative carrying a C-terminal His tag. Native peptidase diffracts to 2.9 A, His-tag peptidase T diffracts to 2.6 A, the selenomethionine derivative of the enzyme does not yield good crystals. His-tag derivatives not only facilitates protein purification but can also result in crystals of improved quality
mutant enzyme requires a concentration of Zn2+ ion at least ten-fold higher to reach maximal activity without significantly affecting kinetic parameters such as Km and Vmax compared to the full length tripeptidase