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Chymotrypsin (EC 3.4.21.1, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the duodenum, where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid N-terminal to the scissile amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their side chain that fits into a hydrophobic pocket (the S1 position) of the enzyme. It is activated in the presence of trypsin. The hydrophobic and shape complementarity between the peptide substrate P1 side chain and the enzyme S1 binding cavity accounts for the substrate specificity of this enzyme. Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine at the P1 position.
A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example is ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis.
Enteropeptidase is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment.
Pepsin B is an enzyme. This enzyme catalyses the following chemical reaction
Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together. Pancreatic elastase 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site. Although the recommended name is pancreatic elastase, it can also be referred to as elastase-1, pancreatopeptidase, PE, or serine elastase.
Endopeptidase Clp (EC 3.4.21.92, endopeptidase Ti, caseinolytic protease, protease Ti, ATP-dependent Clp protease, ClpP, Clp protease). This enzyme catalyses the following chemical reaction
Renal tissue kallikrein is an enzyme.
Carboxypeptidase B is a carboxypeptidase that preferentially cleaves off basic amino acids arginine and lysine from the C-terminus of a peptide. This enzyme is secreted by the pancreas, and it travels to the small intestine, where it aids in protein digestion. Plasma carboxypeptidase B is responsible for converting the C5a protein into C5a des-Arg, with one less amino acid.
In enzymology, a muconolactone Δ-isomerase is an enzyme that catalyzes the chemical reaction
In enzymology, a phosphoacetylglucosamine mutase is an enzyme that catalyzes the chemical reaction
In enzymology, a galactoside 2-alpha-L-fucosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acetylglucosamine kinase is an enzyme that catalyzes the chemical reaction
Subtilases are a family of subtilisin-like serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like in the trypsin serine proteases. The structure of proteins in this family shows that they have an alpha/beta fold containing a 7-stranded parallel beta sheet.
The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A (digestive). Members of the H family have longer C-termini than those of family A, and carboxypeptidase M is bound to the membrane by a glycosylphosphatidylinositol anchor, unlike the majority of the M14 family, which are soluble.
Membrane dipeptidase (EC 3.4.13.19, renal dipeptidase, dehydropeptidase I (DPH I), dipeptidase, aminodipeptidase, dipeptide hydrolase, dipeptidyl hydrolase, nonspecific dipeptidase, glycosyl-phosphatidylinositol-anchored renal dipeptidase, MBD, MDP, leukotriene D4 hydrolase) is an enzyme. This enzyme catalyses the following chemical reaction
Lysosomal Pro-Xaa carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Signal peptidase I is an enzyme. This enzyme catalyses the following chemical reaction
Penicillopepsin is an enzyme. This enzyme catalyses the following chemical reaction
Mucorpepsin is an enzyme. This enzyme catalyses the following chemical reaction
Brian Selby Hartley FRS was a British biochemist. He was Professor of Biochemistry at Imperial College London from 1974 to 1991.
References
- ↑ Peanasky RJ, Gratecos D, Baratti J, Rovery M (May 1969). "Mode of activation of N-terminal sequence of subunit II in bovine procarboxypeptidase A and of porcine chymotrypsinogen C". Biochimica et Biophysica Acta (BBA) - Protein Structure. 181 (1): 82–92. doi:10.1016/0005-2795(69)90229-3. PMID 5792601.
- ↑ Folk, J.E. (1970). "Chymotrypsin C (Porcine pancreas)". Proteolytic Enzymes. Methods in Enzymology. Vol. 19. pp. 109–112. doi:10.1016/0076-6879(70)19008-2. ISBN 9780121818814.
- ↑ Wilcox PE (1970). "Chymotrypsinogens—chymotrypsins". Proteolytic Enzymes. Methods in Enzymology. Vol. 19. pp. 64–108. doi:10.1016/0076-6879(70)19007-0. ISBN 9780121818814.
