Ad
related to: enteropeptidase protein
Search results
Results From The WOW.Com Content Network
Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen ) into its active form trypsin , resulting in the subsequent activation of pancreatic digestive enzymes .
Trypsinogen is activated by enteropeptidase (also known as enterokinase). Enteropeptidase is produced by the mucosa of duodenum and it cleaves the peptide bond of trypsinogen after residue 15, which is a lysine. The N-terminal peptide is discarded, and a slight rearrangement of the folded protein occurs.
Enteropeptidase (also known as enterokinase) is responsible for activating pancreatic trypsinogen into trypsin, which activates other pancreatic zymogens. They are involved in the Krebs and the Cori Cycles and can be synthesized with lipase. Lipid uptake. Lipids are broken down by pancreatic lipase aided by bile, and then diffuse into the ...
Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids. [1]
ClpB (human CLPB "Hsp78", yeast Hsp104) break up insoluble protein aggregates in conjunction with DnaK/Hsp70. They are thought to function by threading client proteins through a small 20 Å (2 nm) pore, thereby giving each client protein a second chance to fold. [8] [9] [10] A member of the ClpA/B family termed ClpV is used in the bacterial ...
53895 Ensembl ENSG00000125656 ENSMUSG00000002660 UniProt Q16740 O88696 RefSeq (mRNA) NM_006012 NM_017393 RefSeq (protein) NP_006003 NP_059089 Location (UCSC) Chr 19: 6.36 – 6.37 Mb Chr 17: 57.3 – 57.3 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse ATP-dependent Clp protease proteolytic subunit (ClpP) is an enzyme that in humans is encoded by the CLPP gene. This protein is an ...
Pancreatic endopeptidase E (EC 3.4.21.70, cholesterol-binding proteinase, proteinase E, cholesterol-binding serine proteinase, pancreatic protease E, pancreatic proteinase E, cholesterol-binding pancreatic proteinase, CBPP, pancreas E proteinase) is an enzyme.
Trypsinogen is an inactive form of trypsin, its inactive form ensures protein aspects of the body, such as the pancreas and muscles, are not broken down. It is formed in the pancreas and activated to trypsin with enteropeptidase [6] Chymotrypsinogen is the inactive form of chymotrypsin and has similar functions as trypsin.