Results 1 to 10 of about 902 (153)

Safety evaluation of the food enzyme prolyl oligopeptidase from the genetically modified <i>Trichoderma reesei</i> strain DP-Nyq99. [PDF]

EFSA J
Abstract The food enzyme prolyl oligopeptidase (EC 3.24.21.26) is produced with the genetically modified Trichoderma reesei strain DP‐Nyq99 by Genencor international B.V. The genetic modifications do not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and its DNA.
EFSA Panel on Food Enzymes (FEZ), Zorn H, Barat Baviera JM, Bolognesi C, Catania F, Gadermaier G, Greiner R, Mayo B, Mortensen A, Roos YH, Solano MLM, Sramkova M, Van Loveren H, Vernis L, Aguilera J, Cavanna D, Fernàndez-Fraguas C, Kovalkovicova N, Lunardi S, Liu Y.   +19 more
europepmc   +4 more sources

Comparative analysis of thermal adaptations of extremophilic prolyl oligopeptidases. [PDF]

Biophys J
Prolyl oligopeptidases from psychrophilic, mesophilic, and thermophilic organisms found in a range of natural environments are studied using a combination of protein structure prediction, atomistic molecular dynamics, and trajectory analysis to determine how the S9 protease family adapts to extreme thermal conditions.
Diessner EM, Takahashi GR, Butts CT, Martin RW.   +3 more
europepmc   +6 more sources

Safety evaluation of the food enzyme prolyl oligopeptidase from the genetically modified <i>Aspergillus niger</i> strain NZYM-MR. [PDF]

EFSA J
Abstract The food enzyme prolyl oligopeptidase (EC 3.4.21.26) is produced with the genetically modified Aspergillus niger strain NZYM‐MR by Novozymes A/S. The genetic modifications do not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and its DNA.
EFSA Panel on Food Enzymes (FEZ), Zorn H, Barat Baviera JM, Bolognesi C, Catania F, Gadermaier G, Greiner R, Mayo B, Mortensen A, Roos YH, Solano MLM, Van Loveren H, Vernis L, Criado A, Aguilera J, Fraguas CF, Tokić V, Liu Y.   +17 more
europepmc   +2 more sources

Kinetic Landscape of a Peptide Bond-Forming Prolyl Oligopeptidase

Biochemistry, 2017
Prolyl oligopeptidase B from Galerina marginata (GmPOPB) has recently been discovered as a peptidase capable of breaking and forming peptide bonds to yield a cyclic peptide. Despite the relevance of prolyl oligopeptidases in human biology and disease, a kinetic analysis pinpointing rate-limiting steps for a member of this enzyme family is not available.
Clarissa Melo Czekster, James H. Naismith   +1 more
openalex   +5 more sources

α/β Hydrolases: Toward Unraveling Entangled Classification. [PDF]

Proteins
ABSTRACT α/β Hydrolase‐like enzymes form a large and functionally diverse superfamily of proteins. Despite retaining a conserved structural core consisting of an eight‐stranded, central β‐sheet flanked with six α‐helices, they display a modular architecture allowing them to perform a variety of functions, like esterases, lipases, peptidases, epoxidases,
Ozhelvaci F, Steczkiewicz K.
europepmc   +2 more sources

Discovery of covalent prolyl oligopeptidase boronic ester inhibitors

European Journal of Medicinal Chemistry, 2019
Over the past decade, many drug discovery endeavors have been invested in targeting the serine proteases prolyl oligopeptidase (POP) for the treatment of Alzheimer's and Parkinson's disease and, more recently, epithelial cancers. Our research group has focused on the discovery of reversible covalent inhibitors, namely nitriles, to target the catalytic ...
Jessica Plescia, Caroline Dufresne, Naëla Janmamode, Alexander S. Wahba, Anthony Mittermaier, Nicolas Moitessier   +5 more
openalex   +4 more sources

Structural visualization of inhibitor binding in prolyl oligopeptidase [PDF]

Biophysics Reviews
The association and dissociation of proteins and ligands are crucial in biophysics for potential drug development [Baron and McCammon, Annu. Rev. Phys. Chem. 64, 151–175 (2013)]. However, identifying and characterizing the reaction pathways for these rare events has been a long-standing challenge.
Katarzyna Walczewska-Szewc, Jakub Rydzewski   +1 more
openalex   +3 more sources

Structure and Localization of the Mouse Prolyl Oligopeptidase Gene [PDF]

Journal of Biological Chemistry, 1999
We have cloned and characterized the genomic structure of the mouse gene for prolyl oligopeptidase that is mapped to chromosome 10B2-B3. The gene is about 92 kilobases in size and contains 15 exons. All exon-intron junction sequences conform to the GT/AG rule.
Atsushi P. Kimura, Ikuya Yoshida, Nobuo Takagi, Takayuki Takahashi   +3 more
openalex   +3 more sources

Inhibition of prolyl oligopeptidase with a synthetic unnatural dipeptide [PDF]

Bioorganic & Medicinal Chemistry, 2010
A new inhibitor, containing a linked proline-piperidine structure, for the enzyme prolyl oligopeptidase (POP) has been synthesised and demonstrated to bind covalently with the enzyme at the active site. This provides evidence that covalent inhibitors of POP do not have to be limited to structures containing five-membered N-containing heterocyclic rings.
Daugirdas T. Racys, Dean Rea, Vilmos Fülöp, Martin Wills   +3 more
openalex   +4 more sources

Synergistic Pulmonoprotective Effect of Natural Prolyl Oligopeptidase Inhibitors in In Vitro and In Vivo Models of Acute Respiratory Distress Syndrome. [PDF]

Int J Mol Sci, 2023
Zerikiotis S, Efentakis P, Dapola D, Agapaki A, Seiradakis G, Kostomitsopoulos N, Skaltsounis AL, Tseti I, Triposkiadis F, Andreadou I.   +9 more
europepmc   +3 more sources