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7px8

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Current revision (05:25, 8 September 2022) (edit) (undo)
 
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== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ACPH_PIG ACPH_PIG]] This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser.
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[[https://www.uniprot.org/uniprot/ACPH_PIG ACPH_PIG]] This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The first structure of tetrameric mammalian acylaminoacyl peptidase, an enzyme that functions as an upstream regulator of the proteasome through the removal of terminal N-acetylated residues from its protein substrates, was determined by cryo-EM and further elucidated by MD simulations. Self-association results in a toroid-shaped quaternary structure, guided by an amyloidogenic beta-edge and unique inserts. With a Pro introduced into its central beta-sheet, sufficient conformational freedom is awarded to the segment containing the catalytic Ser587 that the serine protease catalytic triad alternates between active and latent states. Active site flexibility suggests that the dual function of catalysis and substrate selection are fulfilled by a novel mechanism: substrate entrance is regulated by flexible loops creating a double-gated channel system, while binding of the substrate to the active site is required for stabilization of the catalytic apparatus - as a second filter before hydrolysis. The structure not only underlines that within the family of S9 proteases homo-multimerization acts as a crucial tool for substrate selection, but it will also allow drug design targeting of the ubiquitin-proteasome system.
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Cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multi-state serine-protease triad.,Kiss-Szeman AJ, Straner P, Jakli I, Hosogi N, Harmat V, Menyhard DK, Perczel A Chem Sci. 2022 May 18;13(24):7132-7142. doi: 10.1039/d2sc02276a. eCollection 2022, Jun 22. PMID:35799812<ref>PMID:35799812</ref>
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==See Also==
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*[[Acylaminoacyl peptidase 3D structures|Acylaminoacyl peptidase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7px8" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sus scrofa domesticus]]
[[Category: Sus scrofa domesticus]]
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[[Category: Harmat, V]]
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[[Category: Harmat V]]
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[[Category: Hosogi, N]]
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[[Category: Hosogi N]]
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[[Category: Jakli, I]]
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[[Category: Jakli I]]
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[[Category: Kiss-Szeman, A J]]
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[[Category: Kiss-Szeman AJ]]
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[[Category: Menyhard, D K]]
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[[Category: Menyhard DK]]
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[[Category: Perczel, A]]
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[[Category: Perczel A]]
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[[Category: Straner, P]]
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[[Category: Straner P]]
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[[Category: Aclypeptide-hydrolase]]
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[[Category: Acylaminoacyl-peptidase]]
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[[Category: Hydrolase]]
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[[Category: Oxidized protein hydrolase]]
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[[Category: Serine-protease]]
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[[Category: Tetramer]]
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Current revision

CryoEM structure of mammalian acylaminoacyl-peptidase

PDB ID 7px8

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