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Chymotrypsinogen is a proteolytic enzyme^[1] and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum.^[2]

Activation

Chymotrypsinogen must be inactive until it gets to the digestive tract. This prevents damage to the pancreas or any other organs. It is activated into its active form by another enzyme called trypsin. This active form is called π-Chymotrypsin and is used to create α-Chymotrypsin. Trypsin cleaves the peptide bond in chymotrypsinogen between arginine-15 and isoleucine-16. This creates two peptides within π-chymotrypsin molecule held together by a disulfide bond. One of the π-chymotrypsin acts on another by breaking a leucine and serine peptide bond. The activated π-chymotrypsin reacts with other π-chymotrypsin molecules to cleave out two dipeptides, which are, Serine-14–Arginine-15 and Threonine-147–Asparagine-148.^[3] This reaction yields the α-chymotrypsin.^[4]

References

^ Schwert G.W, Proteolytic Enzymes. Annual Review of Biochemistry. [online] 1955, 10.1146/annurev.bi.24.070155.000503 http://www.annualreviews.org/doi/abs/10.1146/annurev.bi.24.070155.000503?journalCode=biochem (accessed Oct 10, 2012)
^ Berg.M.J.,Tymoczko.L.J.,Stryer.L., Gatto Jr. J.G. Biochemistry, 7th Ed.; Freeman: New York, 2012.
^ Garret, Reginald (2013). Biochemistry. Canada: Mary Finch. p. 484. ISBN 978-1-133-10629-6.
^ Dryer.J.W.,Neurath.H. The Activation of Chemotrypsinogen: ISOLATION AND IDENTIFICATION OF A PEPTIDE LIBERATED DURING ACTIVATION Department of Biochemistry, University of Washington [1955]http://www.jbc.org/content/217/2/527.full.pdf [accessed Oct. 10, 2012]

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1. 小児および思春期における慢性膵炎の原因 causes of chronic pancreatitis in children and adolescents
2. 遺伝性膵炎 hereditary pancreatitis
3. 小児における膵疾患のERCP ercp for pancreatic disease in children

English Journal

In vitro treatment of carcinoma cell lines with pancreatic (pro)enzymes suppresses the EMT programme and promotes cell differentiation.

Perán M, Marchal JA, García MA, Kenyon J, Tosh D.SourceCentre for Regenerative Medicine, Department of Biology & Biochemistry, University of Bath, Bath, UK, mperan@ujaen.es.
Cellular oncology (Dordrecht).Cell Oncol (Dordr).2013 May 16. [Epub ahead of print]
BACKGROUND: Previous research has suggested a putative utility of pancreatic (pro)enzymes in cancer treatment. The aim of the present study was to investigate the in vitro effects of a mixture of two pancreatic pro-enzymes, i.e., Chymotrypsinogen and Trypsinogen, and the enzyme Amylase on three huma
PMID 23677639

The CTRB1/2 locus affects diabetes susceptibility and treatment via the incretin pathway.

't Hart LM, Fritsche A, Nijpels G, van Leeuwen N, Donnelly LA, Dekker JM, Alssema M, Fadista J, Carlotti F, Gjesing AP, Palmer CN, van Haeften TW, Herzberg-Schäfer SA, Simonis-Bik AM, Houwing-Duistermaat JJ, Helmer Q, Deelen J, Guigas B, Hansen T, Machicao F, Willemsen G, Heine RJ, Kramer MH, Holst JJ, de Koning EJ, Häring HU, Pedersen O, Groop L, de Geus EJ, Slagboom PE, Boomsma DI, Eekhoff EM, Pearson ER, Diamant M.SourceDepartment of Molecular Cell Biology, Leiden University Medical Center, Leiden, The Netherlands.
Diabetes.Diabetes.2013 May 14. [Epub ahead of print]
The incretin hormone glucagon-like-peptide 1 (GLP-1) promotes glucose homeostasis and enhances beta-cell function. GLP-1 receptor agonists (GLP-1 RA) and dipeptidyl peptidase-4 (DPP-4) inhibitors, which inhibit the physiological inactivation of endogenous GLP-1, are used for the treatment of type 2
PMID 23674605

Gene expression and activity of digestive enzymes during the larval development of Asian seabass (Lates calcarifer).

Srichanun M, Tantikitti C, Utarabhand P, Kortner TM.SourceDepartment of Aquatic Science, Faculty of Natural Resources, Prince of Songkla University, Hat Yai, Songkhla 90112, Thailand.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.Comp Biochem Physiol B Biochem Mol Biol.2013 May;165(1):1-9. doi: 10.1016/j.cbpb.2013.02.005. Epub 2013 Feb 28.
Knowledge of digestive enzyme development during larval stages provides a better understanding of the digestive and nutritional physiology of fish larvae. This study characterized the ontogeny of key digestive enzymes in Asian seabass larvae from hatching to juvenile stage (30 days post hatch, dph)
PMID 23458902

Japanese Journal

1P014 Effect of methanol on the structure of α-chymotrypsinogen A(01A. Protein:Structure,Poster)

Murayama Koichi
生物物理 53(SUPPLEMENT_1-2), S108, 2013-09-13
NAID 110009819187

カチオン交換ポリマーブラシ搭載粒子および市販カチオン交換ビーズの充填カラムを使った溶出クロマトグラフィーでのタンパク質の分離度の比較

染谷孝明,岡村雄介,和田剛,霜田祐一,梅野太輔,斎藤恭一,篠原直志,久保田昇
日本イオン交換学会誌 24(1), 14-20, 2013
… モデルタンパク質として chymotrypsinogen A, cytochrome C，および lysozyme を，カチオン交換ポリマーブラシ搭載粒子充填カラム（断面積 0.20 cm2，充填高さ 1.5 cm）に負荷し，リン酸緩衝液および 1.0 M NaCl 溶液を用いて勾配溶出をおこなった。 …
NAID 130003375922

1PT187 Gibbs energies of secondary structures for α-Chymotrypsinogen A investigated by FT-IR spectroscopy(The 50th Annual Meeting of the Biophysical Society of Japan)