2019
DOI: 10.2174/1389203720666190925103339
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Achieving Functionality Through Modular Build-up: Structure and Size Selection of Serine Oligopeptidases

Abstract: Enzymes of the prolyl oligopeptidase family (S9 family) recognize their substrates not only by the specificity motif to be cleaved but also by size - they hydrolyze oligopeptides smaller than 30 amino acids. They belong to the serine-protease family, but differ from classical serine-proteases in size (80 kDa), structure (two domains) and regulation system (size selection of substrates). This group of enzymes is an important target for drug design as they are linked to amnesia, schizophrenia, type 2 diabetes, t… Show more

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Cited by 8 publications
(10 citation statements)
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“…The active site with the catalytic Ser/His/Asp triad is buried between the two. 41 The pAAP monomers contain a 7-bladed propeller domain (residues 23-457) that is tilted away from the hydrolase (residues 1-22 and 458-732) by approximately 40 , creating a large opening near the active site beneath blade2 (Fig. 1C) that can be accessed from the central cavity of the tetramer.…”
Section: Paap Monomers Present An Open Structure With a Conformationa...mentioning
confidence: 99%
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“…The active site with the catalytic Ser/His/Asp triad is buried between the two. 41 The pAAP monomers contain a 7-bladed propeller domain (residues 23-457) that is tilted away from the hydrolase (residues 1-22 and 458-732) by approximately 40 , creating a large opening near the active site beneath blade2 (Fig. 1C) that can be accessed from the central cavity of the tetramer.…”
Section: Paap Monomers Present An Open Structure With a Conformationa...mentioning
confidence: 99%
“…Structures of archeal and bacterial AAPs are unfit for model building, since they not only share low sequence identity with the mammalian enzyme (13–20%, Table S1 † ), but also mostly assume different oligomeric forms. 41 …”
Section: Introductionmentioning
confidence: 99%
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“…A number of studies have reported that enzymes employ induced-fit mechanism to form catalytically competent "enzyme•substrate complex" as compared to short-lived, non-productive "enzyme•competitor•ligand" complexes [7,8]. Because substrate-selectivity is a very important property of catalytic activity, active site features of enzymes act like filters to screen and select the cognate-substrate [9,10]. Many enzymes, proteases in particular, have to select their substrates in the presence of natural inhibitors [11,12].…”
Section: Introductionmentioning
confidence: 99%
“…Acylpeptide hydrolase (APH; EC 3.4.19.1), also known as acylaminoacyl‐peptidase (AAP), is a serine protease, which, together with prolyl oligopeptidase (POP), dipeptidyl peptidase IV (DPPIV) and oligopeptidase B (OB), belongs to the prolyl oligopeptidase family (clan SC, family S9) [1–3] . APH primarily removes N‐acetylated amino acids residues and thus regulates the cellular level of N‐terminal acetylation of proteins [4] .…”
Section: Introductionmentioning
confidence: 99%