A zymogen or proenzyme is an inactive enzyme Protein precursor precursor . A zymogen requires a biochemistry biochemical change such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site for it to become an active enzyme. The biochemical change usually occurs in a lysosome where a specific part of the precursor enzyme is cleaved in order to activate it. The amino acid chain that is released upon activation is called the activation peptide . The pancreas secretes zymogens partly to prevent the enzymes from digesting protein s in the Cell biology cells in which they are synthesised. Fungus Fungi also secrete digestive enzyme s into the environment as zymogens. The external environment has a different pH than inside the fungal cell and this changes the zymogen s structure into an active enzyme. Examples Examples of zymogens Angiotensinogen Trypsinogen Chymotrypsinogen Pepsinogen Most proteins in the coagulation coagulation system Some of the proteins of the Complement biology complement system Caspase s Proelastase Prolipase Procarboxypolypeptidases External links wiktionary http webster.com cgi bin dictionary?book Dictionary&va zymogen Webster entry on zymogen Category Enzymes enzyme stub cs Proenzym da Proenzym de Zymogen es Zim geno fr Proenzyme id Zimogen io Zimogeno it Zimogeno he nl Pro enzym ja pl Proenzym pt Zim geno ru sl Proencim uk ... more details
Chymotrypsinogen is a precursor zymogen of the digestive enzyme chymotrypsin . This molecule is inactive and must be cleaved by trypsin , and then by other chymotrypsin molecules, before it can reach its full activity. Its function is to convert protein s to amino acid s. The active site of chymotrypsinogen is covered by a 6 amino acid long mask. It is only when this mask is removed when the chymotrypsinogen molecule enters the lumen of the intestine and comes into contact with chymotrypsin molecules that the enzyme becomes active. This is a very useful safety feature for a protein digesting enzyme. If chymotrypsinogen were not inactivated in this way, it would digest the pancreas , where it is produced. References Unreferenced date January 2009 Category Enzymes enzyme stub ... more details
Trypsinogen EC 3.4.23.18 20 21 23 24 26 is the precursor form or zymogen of the pancreatic enzyme trypsin . It is found in pancreatic juice , along with amylase , lipase , and chymotrypsinogen . It is activated by enteropeptidase , which is found in the intestinal mucosa , to form trypsin . Once activated, the trypsin can activate more trypsinogen into trypsin. Trypsin cleaves peptide bond on carboxyl side of basic amino acid s. blood plasma Serum trypsinogen is measured using a blood test . High levels are seen in acute pancreatitis , and cystic fibrosis . Functions Protein digestion . External links MeshName Trypsinogen hydrolase stub category EC 3.4.23 ar de Trypsinogen pl Trypsynogen pt Tripsinog nio ru sl Tripsinogen ... more details
In general, a chief cell or a zymogen ic cell is a cell which releases a precursor enzyme . There are two types of chief cells which are most commonly referenced A gastric chief cell or peptic cell is a cell in the stomach that releases pepsinogen and rennin . Usually when the term chief cell or zymogenic cell is used without qualification, this is the type meant. This type of cell also secretes gastric lipase enzymes, which help digest triglycerides into free fatty acids and di and mono glycerides. The parathyroid chief cell is the primary cell of the parathyroid gland . It produces and secretes parathyroid hormone . References Unreferenced date April 2009 Category Cell biology cell biology stub fi P solu ... more details
orphan date August 2009 Wikify date August 2009 The pre portion refers to a signal sequence signal peptide which directs the enzyme to a specific organelle or subcellular localization. The pro portion indicates that the enzyme is present in an inactive form and requires modification eg. cleavage for activation. See also Protein precursor Zymogen Sources Braun P, de Groot A, Bitter W, Tommassen J. 1998. Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa . J Bacteriol. 1998 180 13 3467 9. PMID 9642203 Category Enzymes ... more details
Unreferenced date January 2009 The exocrine pancreas has ducts that are arranged in clusters called acini singular acinus . Pancreatic secretions are secreted into the lumen anatomy lumen of the acinus, and then accumulate in intralobular ducts that drain to the main pancreatic duct , which drains directly into the duodenum . Control of the exocrine function of the pancreas is via the hormones gastrin , cholecystokinin and secretin , which are hormone s secreted by cells in the stomach and duodenum , in response to distension and or food and which cause secretion of pancreatic juices. There are two main classes of exocrine pancreatic secretions class wikitable Secretion Cell producing it Primary signal bicarbonate ions Centroacinar cells Secretin digestive enzymes Basophilic cells Cholecystokinin CCK Pancreatic secretions from ductal cells contain bicarbonate ions and are alkaline in order to neutralize the acidic chyme that the stomach churns out. The pancreas is also the main source of enzymes for digesting fat s lipids and proteins . The enzymes that digest polysaccharides , by contrast, are primarily produced by the walls of the intestine s. The cells are filled with secretory granules containing the precursor digestive enzymes. The major proteases which the pancreas secretes are trypsinogen and chymotrypsinogen . Secreted to a lesser degree are pancreatic lipase and pancreatic amylase . The pancreas also secretes phospholipase A2 , lysophospholipase , and cholesterol esterase . It is important to synthesize inactive enzymes in the pancreas to avoid autodegradation, which can lead to pancreatitis . These granules are termed zymogen granules the term zymogen referring to the inactive precursor enzymes . Trypsinogen is an inactivated forms of trypsin , and chymotrypsinogen is an inactivated form of chymotrypsin . Once released in the intestine, the enzyme enteropeptidase formerly, and incorrectly, called enterokinase present in the intestinal mucosa activates tryp ... more details
in pancreatic secretory zymogen granule membranes. journal Proc. Natl. Acad. Sci. U.S.A. volume 88 ... of cDNAs encoding alpha large and beta small isoforms of human pancreatic zymogen granule ... of syncollin with GP 2, the major membrane protein of pancreatic zymogen granules, and association ... structure of GP 2, a glycosylphosphatidylinositol anchored glycoprotein of zymogen granule ... more details
Orphan date February 2009 PBB geneid 123887 Zymogen granule protein 16 , also known as ZG16 , is a human gene . ref name entrez cite web title Entrez Gene ZG16 zymogen granule protein 16 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 123887 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Zhou YB, Cao JB, Yang HM, et al. title hZG16, a novel human secreted protein expressed in liver, was down regulated in hepatocellular carcinoma. journal Biochem. Biophys. Res. Commun. volume 355 issue 3 pages 679 86 year 2007 pmid 17307141 doi 10.1016 j.bbrc.2007.02.020 cite journal author Lim J, Hao T, Shaw C, et al. title A protein protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. journal Cell volume 125 issue 4 pages 801 14 year 2006 pmid 16713569 doi 10.1016 j.cell.2006.03.032 cite journal author Rual JF, Venkatesan K, Hao T, et al. title Towards a proteome scale map of the human protein protein interaction network. journal Nature volume 437 issue 7062 pages 1173 8 year 2005 pmid 16189514 doi 10.1038 nature04209 cite journal author Gerhard DS, Wagner L, Feingold EA, et al. title The status, quality, and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC . journal Genome Res. volume 14 issue 10B pages 2121 7 year 2004 pmid 15489334 doi 10.1101 gr.2596504 pmc 528928 cite journal author Zhang Z, Henzel WJ title Signal peptide prediction based on analysis of experimentally verified cleavage sites. journal Protein Sci. volume 13 issue 10 pages 2819 24 year 2005 pmid 15340161 doi 10.1110 ps.04682504 pmc 2286551 cite journal author Strausberg RL, Feingold EA, Grouse ... of a novel 16 kDa protein located in zymogen granules of rat pancreas and goblet cells of the gut ... more details
Other uses Precursor disambiguation A protein precursor , also called a pro protein or pro peptide , is an inactive protein or peptide that can be turned into an active form by posttranslational modification . The name of the precursor for a protein is often prefixed by pro . Examples include proinsulin and proopiomelanocortin . Protein precursors are often used by an organism when the subsequent protein is potentially harmful, but needs to be available on short notice and or in large quantities. Enzyme precursors are called zymogen s or proenzyme s. Examples are enzymes of the digestive tract in humans. Some protein precursors are secreted from the cell. Many of these are synthesized with an N terminal signal peptide that targets them for secretion. Like other proteins that contain a signal peptide, their name is prefixed by pre . They are thus called pre pro proteins or pre pro peptides . ref name cell cite book author Alberts, Bruce title Molecular biology of the cell publisher Garland Science location New York year 2002 isbn 0 8153 3218 1 oclc doi page 760 ref The signal peptide is cleaved off in the endoplasmic reticulum . ref name cell An example is preproinsulin . References reflist Category Proteins protein stub de Pr kursor Proteine fr Pr curseur prot ique it Precursore nl Prote ne precursor ... more details
in the pancreas. Inhibitors prevent self digestion of the pancreas itself. Zymogen s are the usually ... not occur. Only after activation, during which the conformation and structure of the zymogen change and the active site is opened, can proteolysis occur. class wikitable Zymogen Enzyme Notes Trypsinogen ... from the duodenal mucosa cleaves the lysine 15 isoleucine 16 peptide bond of the zymogen. As a result, the zymogen trypsinogen breaks down into trypsin. Recall that trypsin is also responsible for cleaving ... in cleavage of its own zymogen, generating even more trypsin. The process of trypsin activation ... zymogen is cleaved by trypsin, the newly generated structure called a pi chymotrypsin ... is relatively slow The zymogens are stored in zymogen granules , capsules that have walls that are thought ... more details
mergefrom PLAU date January 2010 drugbox Verifiedfields changed verifiedrevid 398416026 IUPAC name image Caption The protease domain from urokinase in complex with and inhibitor CAS number 9039 53 6 ATC prefix B01 ATC suffix AD04 ATC supplemental PubChem DrugBank BTD00030 KEGG Ref keggcite changed kegg KEGG D03341 C 1376 H 2145 N 383 O 406 S 18 molecular weight 31126.5 g mol bioavailability protein bound metabolism elimination half life pregnancy category legal status routes of administration protein Name plasminogen activator, urokinase caption PLAU image width HGNCid 9052 Symbol PLAU AltSymbols EntrezGene 5328 OMIM 191840 RefSeq NM 002658 UniProt P00749 PDB ECnumber 3.4.21.31 Chromosome 10 Arm q Band 24 LocusSupplementaryData Urokinase trade name Abbokinase , also called urokinase type plasminogen activator uPA , is a serine protease EC number 3.4.21.73 . Urokinase was originally isolated from human urine , but is present in several physiological locations, such as blood stream and the extracellular matrix . The primary physiological substrate is plasminogen , which is an inactive zymogen form of the serine protease plasmin . Activation of plasmin triggers a proteolysis cascade that, depending on the physiological environment, participates in thrombolysis or extracellular matrix degradation. This links urokinase to vascular diseases and cancer. Molecular characteristics Urokinase is a 411 residue chemistry residue protein , consisting of three Domain biology domains the serine protease domain, the kringle domain , and the growth factor domain . Urokinase is synthesized as a zymogen form prourokinase or single chain urokinase , and is activated by proteolytic cleavage between L158 and I159. The two resulting chains are kept together by a disulfide bond. Interaction partners The most important inhibitors of urokinase are the serpin s plasminogen activator inhibitor 1 PAI 1 and plasminogen activator inhibitor 2 PAI 2 , which inhibit the protease activity irreversibly ... more details
An osmoreceptor is a sensory receptor primarily found in the hypothalamus of most homeotherm ic organisms that detects changes in osmotic pressure . Osmoreceptors can be found in several structures, including the organum vasculosum of the lamina terminalis OVLT and the subfornical organ SFO . They contribute to fluid balance in the body. Mechanism in humans Osmoreceptors, as the name suggests, sense change in osmotic pressure. When the osmotic pressure of blood changes i.e. it is more or less dilute , water diffusion into and out of the osmoreceptor cells changes. That is, they expand when the blood plasma is more dilute and contract with higher concentration. This causes an afferent neural signal to be sent to the hypothalamus , which increases or decreases vasopressin ADH secretion from the posterior pituitary to return blood concentration to normal. Macula densa The macula densa region of the kidney s juxtaglomerular apparatus is another modulator of blood osmolality. The macula densa responds to changes in osmotic pressure through changes in the rate of chloride anion flow through the nephron. Increased Cl flow stimulates tubuloglomerular autoregulation, a signal thought to be regulated by adenosine sent to the nearby juxtaglomerular cells of the afferent arteriole, causing the JG cells to release the protease renin into circulation. Renin cleaves the zymogen angiotensinogen , always present in plasma as a result of constitutive production in the liver, into a second inactive form, angiotensin I , which is then converted to its active form, angiotensin II , by angiotensin converting enzyme ACE , which is widely distributed in the small vessels of the body, but particularly concentrated in the pulmonary capillaries of the lungs. Angiotensin II exerts systemwide effects, triggering aldosterone release from the adrenal cortex , direct vasoconstriction , and thirst behaviors originating in the hypothalamus . External links eMedicineDictionary Osmoreceptor See also h ... more details
Infobox Anatomy Name Gastric chief cell Latin GraySubject GrayPage Image Fundic gland polyp 1 .jpg Caption H&E stain of fundic gland polyp showing shortening of the gastric pits with cystic dilatation Image2 Gray1055.png Caption2 A fundus gland. A. Transverse section of gland. Precursor System Artery Vein Nerve Lymph MeshName MeshNumber Dorlands DorlandsID A gastric chief cell or peptic cell , or gastric zymogenic cell is a cell in the stomach that releases pepsinogen , gastric lipase and Chymosin . The cell stains basophilic upon H&E stain H&E prep due to the large proportion of rough endoplasmic reticulum in its cytoplasm . Chief cells release the zymogen pepsinogen when stimulated by a variety of factors including cholinergic activity from the vagus nerve and acidic condition in the stomach. Gastrin and secretin may also act as secretagogues. ref Johnson. Gastrointestinal Physiology 6th Edition. Mosby. 2001 ref It works in conjunction with the parietal cell , which releases gastric acid , converting the pepsinogen into pepsin . Nomenclature The terms chief cell and zymogenic cell are often used without the word gastric to name this type of cell. However those terms can also be used to describe other cell types for example, parathyroid chief cell s. Chief cells are also known as peptic cells. Image Chief cells.JPG thumb left 200px human chief cells See also Gastric acid Fundic glands References reflist External links AnatomyAtlasesMicroscopic 01 05 BUHistology 22201loa Ultrastructure of the Cell chief cells and enteroendocrine cell BUHistology 11304loa Digestive System Alimentary Canal fundic stomach, gastric glands, base DorlandsDict two 000018589 chief cell GeorgiaPhysiology 6 6ch4 s6ch4 8 Gastrointestinal physiology Human cell types derived primarily from endoderm Category Peptide hormone secreting cells Category Human cells es C lula principal ja pt C lula principal ru ... more details
Multiple issues orphan February 2009 context October 2009 unreferenced December 2008 Blastoconidium is a holoblastic conidium that is produced singly or in chains, and detached at maturity leaving a bud scar, as in the budding of a yeast cell . Description Yeasts such as Candida albicans and Cryptococcus neoformans produce budded cells known as blastoconidia. The formation of blastoconidia involves three basic steps bud emergence, bud growth, and conidium separation. During bud emergence, the outer cell wall of the parent cell thins. Concurrently, new inner cell wall material and plasma membrane are synthesized at the site where new growth is occurring. New cell wall material is formed locally by activation of the polysaccharide synthetase zymogen. The process of bud emergence is regulated by the synthesis of these cellular components as well as by the turgor pressure in the parent cell. Mitosis occurs, as the bud grows, and both the developing conidium and the parent cell will contain a single Cell nucleus nucleus . A ring of chitin forms between the developing blastoconidium and its parent yeast cell. This ring grows in to form a septum. Separation of the two cells leaves a bud scar on the parent cell wall. The bud scar contains much more chitin than does the rest of the parent cell wall. When the production of blastoconidia continues without separation of the conidia from each other, a hypha pseudohypha , consisting of a filament of attached blastoconidia, is formed. In addition to budding yeast cells and pseudohyphae, yeasts such as Candida albicans may form true hyphae . Category Fungal morphology and anatomy Yeast stub ... more details
Proteolysis is the directed degradation digestion of protein s by cellular enzyme s called protease s or by intramolecular digestion. Purposes Proteolysis is used by the cell for several purposes. They include Removal of N terminal methionine residues after translation biology translation . Removal of the signal peptide signal sequence of peptides after their transport through a cell membrane membrane Separation of virus biology viral proteins that were translated from a polycistronic mRNA Digestion of proteins from foods as a source of amino acid s Conversion of predecessor proteins proenzyme s, zymogen s, prehormone s into their final structures. Degradation of unneeded or damaged proteins for example cyclins at different stages of the cell cycle . Proteolysis is also used in research and diagnostic applications In gel digestion of proteins after separation by gel electrophoresis for the identification by mass spectrometry . Digestion of proteins in solution for proteomics proteome analysis by liquid chromatography mass spectrometry LC MS . Examples Examples of serine proteases include trypsin chymotrypsin elastase papain Venoms Certain types of venom, such as those produced by venomous snake s, can also cause proteolysis. These venoms are, in fact, complex digestive fluids that begin their work outside of the body. Proteolytic venoms cause a wide range of toxic effects, ref name Hayes WK. 2005. http www.llu.edu llu grad natsci hayes research c venom.html?PHPSESSID 55842bf3eeb83dcdfec66c45b91925fc Research on Biological Roles and Variation of Snake Venoms. Loma Linda University. ref including effects that are Cytotoxin cytotoxic cell destroying Hemotoxin hemotoxic blood destroying Myotoxin myotoxic muscle destroying Hemorrhage hemorrhagic bleeding See also The Proteolysis Map Protomap proteomics PROTOMAP a proteomic technology for identifying proteolytic substrates Proteasome In gel digestion References references External links eMedicineDictionary Proteolysis htt ... more details
Image Mannose structure.png thumb Natta projection of mannose in its small D small mannopyranose form. Mannan is a polymer of mannose. The Mannan binding lectin pathway also known as the Ali Krueger Pathway is similar in structure to the classical complement pathway , ref name pmid19783065 cite journal author Wallis R, Mitchell DA, Schmid R, Schwaeble WJ, Keeble AH title Paths reunited Initiation of the classical and lectin pathways of complement activation journal Immunobiology volume 215 issue 1 pages 1 11 year 2010 pmid 19783065 pmc 2824237 doi 10.1016 j.imbio.2009.08.006 url http linkinghub.elsevier.com retrieve pii S0171 2985 09 00146 6 ref in that, after activation, it proceeds through the action of C4 and C2 to produce activated complement proteins further down the cascade. In contrast to the classical complement pathway , it is not antibody dependent. In this pathway, mannose binding lectin binds to mannose residues on carbohydrate or glycoprotein components of microorganisms including bacteria such as Salmonella , Listeria , and Neisseria strains. Fungal pathogens such as Candida albicans and Cryptococcus neoformans as well as some viruses such as HIV 1 and Respiratory syncytial virus RSV are bound by MBL. Mannan binding lectin MBL, also called mannose binding lectin is a protein belonging to the collectin family that is produced by the liver and can initiate the complement cascade by binding to pathogen surfaces. MBL MBL is a 2 to 6 headed molecule that forms a complex with MASP I M annan binding lectin A ssociated S erine P rotease and MASP II , two protease zymogen s. MASP I and MASP II are very similar to C1r and C1s molecules of the classical complement pathway, respectively, and are thought to have a common evolutionary ancestor. When the carbohydrate recognising heads of MBL bind to specifically arranged mannose residues on the phospholipid bilayer of a pathogen, MASP I and MASP II are activated to cleave complement components Complement component ... more details
PBB geneid 245973 V type proton ATPase subunit C 2 is an enzyme that in humans is encoded by the ATP6V1C2 gene . ref name pmid12384298 cite journal author Smith AN, Borthwick KJ, Karet FE title Molecular cloning and characterization of novel tissue specific isoforms of the human vacuolar H ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis journal Gene volume 297 issue 1 2 pages 169 77 year 2002 month Oct pmid 12384298 pmc doi 10.1016 S0378 1119 02 00884 3 ref ref name entrez cite web title Entrez Gene ATP6V1C2 ATPase, H transporting, lysosomal 42kDa, V1 subunit C2 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 245973 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text This gene encodes a component of vacuolar ATPase V ATPase , a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor mediated endocytosis, and synaptic vesicle proton gradient generation. V ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A,three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. This gene encodes alternate transcriptional splice variants, encoding different V1 domain C subunit isoforms. ref name entrez cite web title Entrez Gene ATP6V1C2 ATPase, H transporting, lysosomal 42kDa, V1 subunit C2 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 245973 accessdate ref References reflist refbegin 2 PBB Further reading citations refend The PBB Controls template provides controls for Protein Box Bot, please see Template PBB Controls for details. PBB Controls update page yes re ... more details
PBB geneid 834 Caspase 1 is an enzyme that proteolysis proteolytically cleaves other proteins, such as the Protein precursor precursor forms of the inflammatory cytokine s interleukin 1 interleukin 1 and interleukin 18 , into active mature peptides. ref cite journal author Thornberry N, Bull H, Calaycay J, Chapman K, Howard A, Kostura M, Miller D, Molineaux S, Weidner J, Aunins J title A novel heterodimeric cysteine protease is required for interleukin 1 beta processing in monocytes journal Nature volume 356 issue 6372 pages 768 74 year 1992 pmid 1574116 doi 10.1038 356768a0 ref It belongs to a family of cysteine protease s known as caspase s that always cleave proteins following an aspartic acid residue. Caspase 1 is produced as a zymogen that is cleaved into 20 kDa p20 and 10 kDa p10 subunits that become part of the active enzyme. Active caspase 1 contains two heterodimer s of p20 and p10. It interacts with another CARD domain containing protein called PYCARD or ASC and is involved in inflammasome formation and activation of inflammation inflammatory processes. ref cite journal author Mariathasan S, Newton K, Monack D, Vucic D, French D, Lee W, Roose Girma M, Erickson S, Dixit V title Differential activation of the inflammasome by caspase 1 adaptors ASC and Ipaf journal Nature volume 430 issue 6996 pages 213 8 year 2004 pmid 15190255 doi 10.1038 nature02664 ref Caspase 1 has been shown to induce cell necrosis or pyroptosis and may function in various developmental stages. Studies of a similar protein in mouse suggest a role in the pathogenesis of Huntington s disease . Alternative splicing of the gene results in five transcript variants encoding distinct isoforms. ref cite web title Entrez Gene CASP1 caspase 1, apoptosis related cysteine peptidase interleukin 1, beta, convertase url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 834 accessdate ref Interactions Caspase 1 has been shown to Protein protein interaction interact with N ... more details
PBB geneid 51032 Chymotrypsin like elastase family member 2B is and enzyme that in humans is encoded by the CELA2B gene . ref name pmid3646943 cite journal author Kawashima I, Tani T, Shimoda K, Takiguchi Y title Characterization of pancreatic elastase II cDNAs two elastase II mRNAs are expressed in human pancreas journal DNA volume 6 issue 2 pages 163 72 year 1987 month April pmid 3646943 doi 10.1089 dna.1987.6.163 url issn ref ref name pmid16327289 cite journal author Szepessy E, Sahin T th M title Inactivity of recombinant ELA2B provides a new example of evolutionary elastase silencing in humans journal Pancreatology volume 6 issue 1 2 pages 117 22 year 2006 pmid 16327289 pmc 1447606 doi 10.1159 000090031 url issn ref ref name entrez cite web title Entrez Gene chymotrypsin like elastase family url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 51032 accessdate ref Function Elastase s form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin . Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Like most of the human elastases, elastase 2B is secreted from the pancreas as a zymogen. In other species, elastase 2B has been shown to preferentially cleave proteins after leucine, methionine, and phenylalanine residues. ref name entrez References reflist Further reading refbegin 2 cite journal author Fletcher TS, Shen WF, Largman C title Primary structure of human pancreatic elastase 2 determined by sequence analysis of the cloned mRNA. journal Biochemistry volume 26 issue 23 pages 7256 61 year 1987 pmid 3427074 doi 10.1021 bi00397a010 cite journal author Strausberg RL, Feingold EA, Grouse LH, et al. title Generation and initial analysis of more than 15,000 full length human and mouse cDNA sequences. journal Proc. Natl. Acad. Sci. U.S.A. volume 99 issue 26 pages 16899 903 year 2002 pmid 12477932 pmc 139241 doi 10.1073 pnas.242603899 cite journal au ... more details
factor B, the major zymogen protease of the alternative complement pathway journal J. Invest ... structure for the zymogen of human complement factor B journal J. Biol. Chem. volume 259 issue 6 ... more details
Encyclopedia
top
