Results 1 to 10 of about 12,284 (148)

Structural Studies of Aspartic Endopeptidase pep2 from Neosartorya Fisherica Using Homolgy Modeling Techniques [PDF]

International Journal on Bioinformatics & Biosciences, 2013
Aspartic endo peptidase pep2 protein of neosartorya fisherica belongs from aspartic acid proteases that depend on aspartic acid residues for their catalytic activity. Catalytic mechanism has been proposed for the hydrolysis of proteins to peptides or free amino acids.
Jehangir, Maryam, Ahmad, Syed Farhan
  +7 more sources

High molecular weight aspartic endopeptidase generates a coronaro‐constrictory peptide from the β‐chain of hemoglobin [PDF]

FEBS Letters, 1993
Studying the influence of brain cathepsin D (EC 3.4.23.5) and high molecular weight (HMW) aspartic endopeptidase (EC 3.4.23.‐) on the processing of hypothalamic calmodulin‐binding coronaro‐constrictory peptide factors from the β‐chain of globin it was found that only HMW aspartic endopeptidase generates the fragment 31–40 of the β‐chain of bovine ...
Barkhudaryan, Nina, Kellermann, Josef, Galoyan, Armen, Lottspeich, Friedrich   +3 more
openaire   +4 more sources

Histidine and Aspartic Acid Residues Important for Immunoglobulin G Endopeptidase Activity of the Group AStreptococcusOpsonophagocytosis-Inhibiting Mac Protein [PDF]

Infection and Immunity, 2003
ABSTRACTThe secreted Mac protein made by serotype M1 group AStreptococcus(GAS) (designated Mac5005) inhibits opsonophagocytosis and killing of GAS by human polymorphonuclear neutrophils. This protein also has cysteine endopeptidase activity against human immunoglobulin G (IgG).
Benfang, Lei, Mengyao, Liu, Elishia G, Meyers, Heather M, Manning, Michael J, Nagiec, James M, Musser   +5 more
openaire   +3 more sources

A novel milk-clotting enzyme from Aspergillus oryzae and A. luchuensis is an aspartic endopeptidase PepE presumed to be a vacuolar enzyme

Bioscience, Biotechnology, and Biochemistry, 2022
ABSTRACT Aspergillus oryzae RIB40 has 11 aspartic endopeptidase genes. We searched for milk-clotting enzymes based on the homology of the deduced amino acid sequence with chymosins. As a result, we identified a milk-clotting enzyme in A. oryzae. We expected other Aspergillus species to have a homologous enzyme with milk-clotting activity,
Yoko, Takyu, Taro, Asamura, Ayako, Okamoto, Hiroshi, Maeda, Michio, Takeuchi, Ken-Ich, Kusumoto, Toru, Katase, Hiroki, Ishida, Mizuki, Tanaka, Youhei, Yamagata   +9 more
openaire   +3 more sources

Aspartic Cathepsin D Endopeptidase Contributes to Extracellular Digestion in Clawed Lobsters Homarus americanus and Homarus gammarus [PDF]

Marine Biotechnology, 2010
Acid digestive proteinases were studied in the gastric fluids of two species of clawed lobster (Homarus americanus and Homarus gammarus). An active protein was identified in both species as aspartic proteinase by specific inhibition with pepstatin A. It was confirmed as cathepsin D by mass mapping, N-terminal, and full-length cDNA sequencing.
Rojo-Arreola, L. C., Muhlia-Almazan, A., Saborowski, Reinhard, Garcia-Carreno, F. L.   +3 more
openaire   +4 more sources

Analysis of toxicity and mechanisms of aspartame in kidney stones with network toxicology and molecular docking strategy [PDF]

Scientific Reports
Aspartame, an artificial sweetener, has been implicated in the formation of kidney stones, although the underlying mechanisms remain poorly understood.
Kailiang Xu, Qiuqiu Zhang, Zhihao Shen, Jinmin Zeng, Yixiang Liao   +4 more
doaj   +2 more sources

Comprehensive bioinformatics-based annotation and functional characterization of bovine chymosin protein revealed novel biological insights [PDF]

Food Chemistry: Molecular Sciences
Chymosin, an aspartic protease present in the stomachs of young ruminants like cows (bovine), causes milk coagulation and cheese production through the breakdown of κ-casein peptide bonds at the Met105-Phe106 site. Bovine chymosin is first synthesized as
Hafsa Amjad, Faiza Saleem, Munir Ahmad, Uzma Nisar, Hamza Arshad Dar   +4 more
doaj   +2 more sources

Safety evaluation of the thermolabile form of the food enzyme mucorpepsin from Rhizomucor miehei strain MMR 164

EFSA Journal, 2022
The food enzyme mucorpepsin (aspartic endopeptidase, EC 3.4.23.23) is produced with the non‐genetically modified microorganism Rhizomucor miehei strain MMR 164.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Boet Glandorf, Lieve Herman, Jaime Aguilera, Magdalena Andryskiewicz, Davide Arcella, Natália Kovalkovičová, Yi Liu, Joaquim Maia, Sandra Rainieri, Andrew Chesson   +26 more
doaj   +1 more source

Safety evaluation of the food enzyme mucorpepsin from Rhizomucor miehei strain DSM 29547

EFSA Journal, 2022
The food enzyme mucorpepsin (EC 3.4.23.23) is produced with the non‐genetically modified Rhizomucor miehei strain DSM 29547 by Chr. Hansen. The food enzyme is free from viable cells of the production organism.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (EFSA CEP Panel), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Lieve Herman, Joaquim Maia, Natalia Kovalkovicova, Simone Lunardi, Yi Liu, Andrew Chesson   +22 more
doaj   +1 more source

Safety evaluation of the native and thermolabile forms of the food enzyme mucorpepsin from Rhizomucor miehei strain MMR 164

EFSA Journal, 2022
The food enzyme mucorpepsin (aspartic endopeptidase, EC 3.4.23.23) is produced with the non‐genetically modified microorganism Rhizomucor miehei strain MMR 164 by Takabio. The enzyme is chemically modified to produce a thermolabile form.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Boet Glandorf, Lieve Herman, Jaime Aguilera, Magdalena Andryskiewicz, Davide Arcella, Natália Kovalkovičová, Yi Liu, Joaquim Maia, Sandra Rainieri, Andrew Chesson   +26 more
doaj   +1 more source