Results 11 to 20 of about 717 (174)

Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP. [PDF]

Nat Commun
Chagas disease, caused by the protozoan parasite Trypanosoma cruzi, remains a significant global public health concern. Despite its profound health impact in both endemic and non-endemic areas, no vaccine is available, and the existing therapies are ...
Batra S, Olmo F, Ragan TJ, Kaplan M, Calvaresi V, Frank AM, Lancey C, Assadipapari M, Ying C, Struwe WB, Hesketh EL, Kelly JM, Barfod L, Campeotto I.   +13 more
europepmc   +5 more sources

Structural and time-resolved mechanistic investigations of protein hydrolysis by the acidic proline-specific endoprotease from Aspergillus niger. [PDF]

Protein Sci
Proline-specific endoproteases have been successfully used in, for example, the in-situ degradation of gluten, the hydrolysis of bitter peptides, the reduction of haze during beer production, and the generation of peptides for mass spectroscopy and ...
Pijning T, Vujičić-Žagar A, van der Laan JM, de Jong RM, Ramirez-Palacios C, Vente A, Edens L, Dijkstra BW.   +7 more
europepmc   +3 more sources

Macrocyclization of backbone <i>N</i>-methylated peptides by a prolyl oligopeptidase with a distinctive substrate recognition mechanism. [PDF]

Chem Sci
Macrocyclization and multiple backbone N-methylations can significantly improve the pharmacological properties of peptides. Since chemical synthesis of such compounds is often challenging, enzyme-based production platforms are an interesting option. Here,
Matabaro E, Song H, Sonderegger L, Gherlone F, Giltrap AM, Liver S, Gossert AD, Künzler M, Naismith JH.   +8 more
europepmc   +3 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

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   +2 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

Crystal structures of trypanosoma brucei oligopeptidase B broaden the paradigm of catalytic regulation in prolyl oligopeptidase family enzymes [PDF]

, 2013
Oligopeptidase B cleaves after basic amino acids in peptides up to 30 residues. As a virulence factor in bacteria and trypanosomatid pathogens that is absent in higher eukaryotes, this is a promising drug target.
Canning, Peter, Fülöp, Vilmos, Morty, Rory E., Rea, Dean   +3 more
core   +8 more sources

Catalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionality [PDF]

, 2015
Acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments. In the case of AAP fromAeropyrum pernix(ApAAP), previous studies have led to a model in which the clamshell-like opening and closing of the enzyme ...
Harmat, Veronika, Karancsiné Menyhárd, Dóra, Orgován, Z., Szamosi, Ildikó, Szeltner, Zoltán   +4 more
core   +2 more sources

Structure and Function Relationship in Prolyl Oligopeptidase [PDF]

CNS & Neurological Disorders - Drug Targets, 2011
Prolyl oligopeptidase (POP) belongs to a unique class of serine proteases. Based on extensive enzyme kinetic measurements it has become clear that POP acts in a multifaceted way. This is reflected in the complex behavior in different reaction conditions with different substrates.
Elzen, Roos, Lambeir, Anne-marie
openaire   +2 more sources

A self-compartmentalizing hexamer serine protease from Pyrococcus Horikoshii: Substrate selection achieved through multimerization [PDF]

, 2013
Oligopeptidases impose a size limitation on their substrates, the mechanism of which has long been in debate. Here we present the structure of a hexameric serine protease, an oligopeptidase from Pyrococcus horikoshii (PhAAP), revealing a complex, self ...
Aertgeerts, Afonine, Anna Kiss-Szemán, Balázs Hornung, Biswal, Bjelkmar, Bosch, Cha, Chen, Chiti, Clark, Collaborative Computational Project, Number 4, Cowtan, Dobson, Duysen, Dóra K. Menyhárd, Eldrup, Emsley, Engel, Engel, Erlandsson, Franken, Fuxreiter, Fülöp, Goettig, Gábor Náray-Szabó, Harmat, Hess, Hiramatsu, Hofmann, Ilona Szamosi, Joshua-Tor, Juhász, Kabsch, Kim, Kim, Kiss, Kiss, Klarissza Domokos, Krisztina Rádi, Li, László Polgár, Mackerell, Maurer-Stroh, McLuskey, Medrano, Monincová, Monsellier, Murshudov, Naylor, Palmieri, Pathak, Polgár, Prokop, Richards, Richardson, Rould, Scaloni, Schmidt, Shan, Shan, Sheldrick, Soldi, Stefani, Szeltner, Szeltner, Szeltner, Thoms, Vagin, Vaguine, Veronika Harmat, Zhang, Zoltán Szeltner, Éva Tichy-Rács   +73 more
core   +1 more source