Results 11 to 20 of about 51,805 (174)

Plant subtilases as key initiators of peptide ligand-receptor signaling. [PDF]

Plant J
SUMMARY Peptide ligand‐receptor signaling plays a crucial role in regulating diverse biological processes in plants. Over the past three decades, numerous peptide ligands and their corresponding receptors have been identified, and our understanding of their downstream signaling pathways and biological functions has gradually advanced.
Matsui S, Hirakawa Y.
europepmc   +2 more sources

Safety evaluation of the food enzyme aspergillopepsin I from the genetically modified <i>Trichoderma reesei</i> strain DP-Nzq40. [PDF]

EFSA J
Abstract The food enzyme aspergillopepsin I (EC 3.4.23.18) is produced with the genetically modified microorganismTrichoderma reesei strain DP‐Nzq40 by Danisco US Inc. The genetic modifications do not give rise to safety concerns. The food enzyme is 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, Aguilera J, Andryszkiewicz M, Cavanna D, Liu Y.   +16 more
europepmc   +2 more sources

Safety evaluation of a food enzyme containing leucyl aminopeptidase, oryzin and aspergillopepsin I from the non-genetically modified <i>Aspergillus</i> sp. strain AE-PR. [PDF]

EFSA J
Abstract The food enzyme containing leucyl aminopeptidase (EC 3.4.11.1), oryzin (EC 3.4.21.63) and aspergillopepsin I (EC 3.4.23.18) activities is produced with the non‐genetically modified Aspergillus sp. strain AE‐PR by Amano Enzyme Inc. The food enzyme was considered free from viable cells of the production organism.
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, Lunardi S, Andryszkiewicz M, Cavanna D, Kovalkovicova N, Liu Y.   +17 more
europepmc   +2 more sources

Safety evaluation of the food enzyme abstract aspergillopepsin I from the non-genetically modified <i>Aspergillus niger</i> strain CCTCC M 2023234. [PDF]

EFSA J
Abstract The food enzyme aspergillopepsin I (EC 3.4.23.18) is produced with the non‐genetically modified Aspergillus niger strain CCTCC M 2023234 by Suntaq International Limited. The food enzyme was free from viable cells of the production organism. The food enzyme is intended to be used in eight food manufacturing processes.
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, Andryszkiewicz M, Liu Y.   +14 more
europepmc   +2 more sources

Cathepsin E (EC 3.4.23.34) &#8212; a review

Folia Histochemica et Cytobiologica, 2012
Cathepsin E belongs to the third class of enzymes &#8212; hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites. Cathepsin E is an endopeptidase with substrate specificity similar to that
Anna Worowska, Marek Gacko, Michał Chlabicz, Radosław Łapiński   +3 more
doaj   +1 more source

Purification and characterization of an aspartic protease from the Rhizopus oryzae protease extract, Peptidase R

Electronic Journal of Biotechnology, 2014
Background: Aspartic proteases are a subfamily of endopeptidases that are useful in a variety of applications, especially in the food processing industry.
Nai-Wan Hsiao, Yeh Chen, Yi-Chia Kuan, Yen-Chung Lee, Shuo-Kang Lee, Hsin-Hua Chan, Chao-Hung Kao   +6 more
doaj   +1 more source

Positional scanning and computational modeling reveal determinants of legumain transpeptidase activity. [PDF]

Protein Sci
Abstract Legumain is a lysosomal cysteine protease that plays a central role in antigen processing for MHC class II presentation. Beyond its canonical proteolytic activity, legumain can also function as a peptide ligase or transpeptidase. This non‐canonical activity becomes particularly relevant under pathophysiological conditions such as cancer and ...
Klaushofer R, Dahms SO, Brandstetter H, Dall E.   +3 more
europepmc   +2 more sources

Enzyme contribution of non-Saccharomyces yeasts to wine production [PDF]

, 2015
The fermentation of grape must to produce wine is a biologically complex process, carried on by yeasts and malolactic bacteria. The yeasts present in spontaneous fermentation may be divided into two groups, the Saccharomyces yeasts, particularly S ...
Maicas i Prieto, Sergi, Mateo Tolosa, José Juan   +1 more
core   +2 more sources

Family C1 cysteine proteases: Biological diversity or redundancy? [PDF]

, 2003
Recent progress in the identification and partial characterization of novel genes encoding cysteine proteases of the papain family has considerably increased our knowledge of this family of enzymes.
Brömme D., Coulombe R., Musil D., Navab R., Tepel C.   +4 more
core   +1 more source

The genome of Strongyloides spp. gives insights into protein families with a putative role in nematode parasitism [PDF]

, 2016
SUMMARYParasitic nematodes are important and abundant parasites adapted to live a parasitic lifestyle, with these adaptations all aimed at facilitating their survival and reproduction in their hosts.
Hunt, Vicky L, Selkirk, Murray E, Tsai, Isheng J, Viney, Mark   +3 more
core   +2 more sources