chymotrypsinogen B1
Identifiers
Symbol(s)	CTRB1 CTRB
Entrez	1504
OMIM	118890
RefSeq	NM_001906
UniProt	P17538
Other data
EC number	3.4.21.1
Locus	Chr. 16 q23.1

Chymotrypsin (bovine γ chymotrypsin: PDB 1AB9, EC 3.4.21.1) is a digestive enzyme that can perform proteolysis. Chymotrypsin cleaves peptides at the carboxyl side of tyrosine, tryptophan, and phenylalanine, although over time it also hydrolyzes other amide bonds, particularly those with leucine-donated carboxyls. Image File history File links 1AB9. ... Hugo is a masculine name. ... The Entrez logo The Entrez Global Query Cross-Database Search System allows access to databases at the National Center for Biotechnology Information (NCBI) website. ... The Mendelian Inheritance in Man project is a database that catalogues all the known diseases with a genetic component, and - when possible - links them to the relevant genes in the human genome. ... The National Center for Biotechnology Information (NCBI) is part of the US National Library of Medicine (NLM), which is a branch of the US National Institutes of Health. ... Swiss-Prot is a curated biological database of protein sequences created in 1986 by Amos Bairoch during his PhD and developed by the Swiss Institute of Bioinformatics and the European Bioinformatics Institute. ... The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. ... Short and long arms Chromosome. ... Chromosome 16 is one of the 23 pairs of chromosomes in humans. ... Hugo is a masculine name. ... The Entrez logo The Entrez Global Query Cross-Database Search System allows access to databases at the National Center for Biotechnology Information (NCBI) website. ... The National Center for Biotechnology Information (NCBI) is part of the US National Library of Medicine (NLM), which is a branch of the US National Institutes of Health. ... Swiss-Prot is a curated biological database of protein sequences created in 1986 by Amos Bairoch during his PhD and developed by the Swiss Institute of Bioinformatics and the European Bioinformatics Institute. ... Short and long arms Chromosome. ... Chromosome 16 is one of the 23 pairs of chromosomes in humans. ... Hugo is a masculine name. ... The Entrez logo The Entrez Global Query Cross-Database Search System allows access to databases at the National Center for Biotechnology Information (NCBI) website. ... The Mendelian Inheritance in Man project is a database that catalogues all the known diseases with a genetic component, and - when possible - links them to the relevant genes in the human genome. ... The National Center for Biotechnology Information (NCBI) is part of the US National Library of Medicine (NLM), which is a branch of the US National Institutes of Health. ... Swiss-Prot is a curated biological database of protein sequences created in 1986 by Amos Bairoch during his PhD and developed by the Swiss Institute of Bioinformatics and the European Bioinformatics Institute. ... Short and long arms Chromosome. ... Chromosome 1 is, by convention, the designation for the largest human chromosome. ... The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. ... The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. ... Proteolysis is the directed degradation (digestion) of proteins by cellular enzymes called proteases or by intramolecular digestion. ... Tyrosine (from the Greek tyros, meaning cheese, as it was first discovered in cheese), 4-hydroxyphenylalanine, or 2-amino-3(4-hydroxyphenyl)-propanoic acid, is one of the 20 amino acids that are used by cells to synthesize proteins. ... Tryptophan is an amino acid and essential in human nutrition. ... It has been suggested that DL-Phenylalanine be merged into this article or section. ... Leucine is one of the 20 most common amino acids and coded for by DNA. It is isomeric with isoleucine. ...

Activation of chymotrypsin

Chymotrypsin is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive. On cleavage by trypsin into two parts that are still connected via an S-S bond, cleaved chymotrypsinogen molecules can activate each other by removing two small peptides in a trans-proteolysis. The resulting molecule is active chymotrypsin, a three polypeptide molecule interconnected via disulfide bonds. For the song by Weird Al Yankovic, see Pancreas (song) The pancreas is an organ in the digestive and endocrine system that serves two major functions: exocrine (producing pancreatic juice containing digestive enzymes) and endocrine (producing several important hormones, including insulin). ... An overview of protein synthesis. ... A precursor is something that existed before and was incorporated into something that came later. ... Chymotrypsinogen is a precursor of the digestive enzyme chymotrypsin (zymogen). ... Trypsin (EC 3. ... Peptides (from the Greek πεπτος, digestible), are the family of short molecules formed from the linking, in a defined order, of various α-amino acids. ... In chemistry, a disulfide bond is a single covalent bond derived from the coupling of thiol groups. ...

Action and Kinetics of chymotrypsin

In vivo, chymotrypsin is a proteolytic enzyme acting in the digestive systems of mammals and other organisms. It facilitates the cleavage of peptide bonds by a hydrolysis reaction, a process which albeit thermodynamically favourable, occurs extremely slowly in the absence of a catalyst. The main substrates of chymotrypsin include tryptophan, tyrosine, phenylalanine, leucine, and methionine, which are cleaved at the carboxyl terminal. Like many proteases, chymotrypsin will also hydrolyse ester bonds in vitro, a virtue that enabled the use of substrate analogs such as N-acetyl-L-phenylalanine p-nitrophenyl ester for enzyme assays. Hydrolysis is a chemical reaction or process in which a molecule is split into two parts by reacting with a molecule of water, which has the chemical formula H2O. One of the parts gets an OH- from the water molecule and the other part gets an H+ from the water. ...

Chymotrypsin cleaves peptide bonds by attacking the unreactive carbonyl group with a powerful nucleophile, the serine 195 residue located in the active site of the enzyme, which briefly becomes covalently bonded to the substrate, forming an enzyme-substrate intermediate.

These findings rely on inhibition assays and the study of the kinetics of cleavage of the aforementioned substrate, exploiting the fact that the enzyme-substrate intermediate p-nitrophenolate has a yellow colour, enabling us to measure its concentration by measuring light absorbance at A400.

It was found that the reaction of chymotrypsin with its substrate takes place in two stages, an initial “burst” phase at the beginning of the reaction and a steady-state phase following Michaelis-Menten kinetics. The mode of action of chymotrypsin explains this as hydrolysis takes place in two steps. First acylation of the substrate to form an acyl-enzyme intermediate and then deacylation in order to return the enzyme to its original state. Michaelis-Menten kinetics describes the kinetics of many enzymes. ...

References

• Stryer et. al. (2002). Biochemistry (5th ed.). New York: Freeman. ISBN 0-7167-4684-0.
• Garrett & Grisham. (2004). Biochemistry (3rd ed.). Brooks Cole. ISBN 0-534-49033-6.