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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.
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.
Tissue kallikrein is an enzyme. This enzyme catalyses the following chemical reaction
Carboxypeptidase B is a carboxypeptidase that preferentially acts upon basic amino acids, such as arginine and lysine. This serum enzyme is also responsible for rapidly metabolizing the C5a protein into C5a des-Arg, with one less amino acid.
In enzymology, a phenylacetaldehyde dehydrogenase (EC 1.2.1.39) is an enzyme that catalyzes the chemical reaction
In enzymology, a cysteamine dioxygenase (EC 1.13.11.19) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-carboxy-cis,cis-muconate cycloisomerase is an enzyme that catalyzes the chemical reaction
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 beta-aspartyl-N-acetylglucosaminidase (EC 3.2.2.11) is an enzyme that catalyzes the chemical reaction
In enzymology, an O-acetylhomoserine aminocarboxypropyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a poly(ribitol-phosphate) N-acetylglucosaminyl-transferase is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acetylglucosamine kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a pyruvate, water dikinase (EC 2.7.9.2) is an enzyme that catalyzes the chemical reaction
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.
Amylo-α-1,6-glucosidase is an enzyme with systematic name glycogen phosphorylase-limit dextrin 6-α-glucohydrolase. It catalyses the hydrolysis of unsubstituted glucose units in glycogen linked by α(1→6) bonds to α(1→4)glucose chains.
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
Mucorpepsin is an enzyme. This enzyme catalyses the following chemical reaction
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)". Methods Enzymol. Methods in Enzymology. 19: 109–112. doi:10.1016/0076-6879(70)19008-2. ISBN 9780121818814.
- ↑ Wilcox PE (1970). "Chymotrypsinogens - chymotrypsins". Methods Enzymol. Methods in Enzymology. 19: 64–108. doi:10.1016/0076-6879(70)19007-0. ISBN 9780121818814.
