Alpha - amylase - wikipedia Alpha - amylase Alpha - amylase Human salivary amylase : calcium ion visible in pale khaki, chloride ion in green. PDB 1SMD Identifiers EC number 3.2. 1.1 CAS number 9000 - 90 - 2 Databases IntEnz IntEnz view BRENDA BRENDA entry ExPASy NiceZyme view KEGG KEGG entry MetaCyc metabolic pathway PRIAM profile PDB structures RCSB PDB PDBe PDBsum Search PMC articles PubMed articles NCBI proteins Alpha - amylase catalytic domain Cyclodextrin glucanotransferase ( e.c. 2.4. 1.19 ) ( cgtase ) Identifiers Symbol Alpha - amylase Pfam PF00128 Pfam clan CL0058 InterPro IPR006047 SCOP 1ppi SUPERFAMILY 1ppi OPM superfamily 125 OPM protein 1wza CAZy GH13 Available protein structures : Pfam structures PDB RCSB PDB ; PDBe ; PDBj PDBsum structure summary Alpha - amylase C - terminal beta - sheet domain Crystal structure of barley alpha - amylase isozyme 1 ( amy1 ) inactive mutant d180a in complex with maltoheptaose Identifiers Symbol Alpha - amyl_C2 Pfam PF07821 InterPro IPR012850 Available protein structures : Pfam structures PDB RCSB PDB ; PDBe ; PDBj PDBsum structure summary Alpha amylase, C - terminal all - beta domain maltotriose complex of preconditioned cyclodextrin glycosyltransferase mutant Identifiers Symbol Alpha - amylase_C Pfam PF02806 Pfam clan CL0369 InterPro IPR006048 SCOP 1ppi SUPERFAMILY 1ppi Available protein structures : Pfam structures PDB RCSB PDB ; PDBe ; PDBj PDBsum structure summary α - Amylase is a protein enzyme EC 3.2. 1.1 that hydrolyses alpha bonds of large, alpha - linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Contents 1 In human physiology 1.1 Salivary amylase ( ptyalin ) 1.1. 1 Optimum conditions for ptyalin 1.2 Genetic variation in human salivary amylase 1.2. 1 Pancreatic amylase 1.3 In pathology 1.3. 1 Interpretation 1.4 Genes 2 In grain 3 Industrial use 4 Potential for medical use 5 Buffer inhibition 6 Determination 7 Domain architecture 8 See also 9 References 10 External links In human Physiology Although found in many tissues, amylase is most prominent in pancreatic juice and saliva, each of which has its own isoform of human α - amylase. They behave differently on isoelectric focusing, and can also be separated in testing by using specific monoclonal antibodies. In humans, all amylase isoforms link to chromosome 1p 21 ( see AMY1A ). Salivary amylase ( ptyalin ) Amylase is found in saliva and breaks starch into maltose and dextrin. This form of amylase is also called `` ptyalin '' / ˈtaɪəlɪn / It will break large, insoluble starch molecules into soluble starches ( amylodextrin, erythrodextrin, and achrodextrin ) producing successively smaller starches and ultimately maltose. Ptyalin acts on linear α ( 1, 4 ) glycosidic linkages, but compound hydrolysis requires an enzyme that acts on branched products. Salivary amylase is inactivated in the stomach by gastric acid. In gastric juice adjusted to pH 3.3, ptyalin was totally inactivated in 20 minutes at 37 ° C. In contrast, 50 % of amylase activity remained after 150 minutes of exposure to gastric juice at pH 4.3. Both starch, the substrate for ptyalin, and the product ( short chains of glucose ) are able to partially protect it against inactivation by gastric acid. Ptyalin added to buffer at pH 3.0 underwent complete inactivation in 120 minutes ; however, addition of starch at a 0.1 % level resulted in 10 % of the activity remaining, and similar addition of starch to a 1.0 % level resulted in about 40 % of the activity remaining at 120 minutes. Optimum conditions for ptyalin Optimum pH -- 7.0 Human body temperature Presence of certain anions and activators : Chloride and bromide -- most effective Iodide -- less effective Sulfate and phosphate -- least effective Genetic variation in human salivary amylase The salivary amylase gene has undergone duplication during evolution, and DNA hybridization studies indicate many individuals have multiple tandem repeats of the gene. The number of gene copies correlates with the levels of salivary amylase, as measured by protein blot assays using antibodies to human amylase. Gene copy number is associated with apparent evolutionary exposure to high - starch diets. For example, a Japanese individual had 14 copies of the amylase gene ( one allele with 10 copies, and a second allele with four copies ). The Japanese diet has traditionally contained large amounts of rice starch. In contrast, a Biaka individual carried six copies ( three copies on each allele ). The Biaka are rainforest hunter - gatherers who have traditionally consumed a low - starch diet. Perry and colleagues speculated the increased copy number of the salivary amylase gene may have enhanced survival coincident to a shift to a starchy diet during human evolution. Pancreatic amylase Pancreatic α - amylase randomly cleaves the α ( 1 - 4 ) glycosidic linkages of amylose to yield dextrin, maltose, or maltotriose. It adopts a double displacement mechanism with retention of anomeric configuration. In pathology The test for amylase is easier to perform than that for lipase, making it the primary test used to detect and monitor pancreatitis. Medical laboratories will usually measure either pancreatic amylase or total amylase. If only pancreatic amylase is measured, an increase will not be noted with mumps or other salivary gland trauma. However, because of the small amount present, timing is critical when sampling blood for this measurement. Blood should be taken soon after a bout of pancreatitis pain, otherwise it is excreted rapidly by the kidneys. Salivary α - amylase has been used as a biomarker for stress and as a surrogate marker of sympathetic nervous system ( SNS ) activity that does not require a blood draw. Interpretation Increased plasma levels in humans are found in : Salivary trauma ( including anaesthetic intubation ) Mumps -- due to inflammation of the salivary glands Pancreatitis -- because of damage to the cells that produce amylase Renal failure -- due to reduced excretion Total amylase readings of over 10 times the upper limit of normal ( ULN ) are suggestive of pancreatitis. Five to 10 times the ULN may indicate ileus or duodenal disease or renal failure, and lower elevations are commonly found in salivary gland disease. Genes salivary -- AMY1A, AMY1B, AMY1C pancreatic -- AMY2A, AMY2B In grain α - Amylase activity in grain is measured by, for instance, the Hagberg - Perten Falling Number, a test to assess sprout damages, or the Phadebas method. Industrial use α - Amylase is used in ethanol production to break starches in grains into fermentable sugars. The first step in the production of high - fructose corn syrup is the treatment of cornstarch with α - amylase, producing shorter chains of sugars oligosaccharides. An α - amylase called `` Termamyl '', sourced from Bacillus licheniformis, is also used in some detergents, especially dishwashing and starch - removing detergents. See amylase for more uses of the amylase family in general. Potential for Medical use α - Amylase has exhibited efficacy in degrading polymicrobial bacterial biofilms by hydrolyzing the α ( 1 - 4 ) glycosidic linkages within the structural, matrix exopolysaccharides of the extracellular polymeric substance ( EPS ). Buffer inhibition The tris molecule is reported to inhibit a number of bacterial α - amylases, so they should not be used in tris buffer. Determination Several methods are available for determination of α - amylase activity, and different industries tend to rely on different methods. The starch iodine test, a development of the iodine test, is based on colour change, as α - amylase degrades starch and is commonly used in many applications. A similar but industrially produced test is the Phadebas amylase test, which is used as a qualitative and quantitative test within many industries, such as detergents, various flour, grain, and malt foods, and forensic biology. Domain architecture α - Amylases contain a number of distinct protein domains. The catalytic domain has a structure consisting of an eight - stranded alpha / beta barrel that contains the active site, interrupted by a ~ 70 - amino acid calcium - binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl - terminal Greek key beta - barrel domain. Several alpha - amylases contain a beta - sheet domain, usually at the C terminus. This domain is organised as a five - stranded antiparallel beta - sheet. Several alpha - amylases contain an all - beta domain, usually at the C terminus. See also Digestive enzyme References Jump up ^ Ramasubbu, N. ; Paloth, V. ; Luo, Y. ; Brayer, G.D. ; Levine, M.J. ( 1996 ). `` Structure of Human Salivary α - Amylase at 1.6 Å Resolution : Implications for its Role in the Oral Cavity ''. Acta Crystallographica Section D. 52 ( 3 ) : 435 -- 446. PMID 15299664. doi : 10.1107 / S0907444995014119. Jump up ^ Maureen Barlow Pugh, ed. ( 2000 ). Stedman 's Medical Dictionary ( 27th ed. ). Baltimore, Maryland, USA : Lippincott Williams & Wilkins. p. 65. ISBN 978 - 0 - 683 - 40007 - 6. Jump up ^ Voet, D., & Voet, J.G. ( 2005 ). Biochimie. ( 2e éd. ). Bruxelles : De Boeck. 1583 p. Jump up ^ which was named by Swedish chemist Jöns Jacob Berzelius. The name derives from the Greek word πτυω ( I spit ), because the substance was obtained from saliva. See : J. Berzelius ( Ms. Esslinger, trans. ), Traité de Chimie ( Paris, France : Firmin Didot Frerès, 1833 ), vol. 7, page 156. Jump up ^ Fried, M, Abramson, S, Meyer, JH. Passage of salivary amylase through the stomach in humans. Digestive Diseases and Sciences 32 : 1097 - 1103 ( 1987 ). Jump up ^ Rosenblum, JL, Irwin, CI, Alpers, DH. Starch and glucose oligosaccharides protect salivary - type amylase activity at acid pH. American Journal of Physiology 254 ( Gastrointestinal and Liver Physiology 17 ) : G775 - 780 ( 1988 ). Jump up ^ http://www.worthington-biochem.com/aa/ Jump up ^ Perry, GH, et al. Diet and evolution of human amylase gene copy number variation, Nature Genetics 39 : 1256 - 1260 ( 2007 ). Jump up ^ Noto, Yuka ; Tetsumi Sato ; Mihoko Kudo ; Kiyoshi Kurata ; Kazuyoshi Hirota ( December 2005 ). `` The Relationship Between Salivary Biomarkers and State - Trait Anxiety Inventory Score Under Mental Arithmetic Stress : A Pilot Study ''. Anesthesia & Analgesia. United States : Lippincott Williams & Wilkins. 101 ( 6 ) : 1873 -- 6. PMID 16301277. doi : 10.1213 / 01. ANE. 0000184196.60838. 8D. Retrieved 1 November 2013. Jump up ^ Granger, Douglas A. ; Kivlighan, Katie T. ; el - Sheikh, Mona ; Gordis, Elana B. ; Stroud, Laura R. ( 2007 - 03 - 01 ). `` Salivary alpha - amylase in biobehavioral research : recent developments and applications ''. Annals of the New York Academy of Sciences. 1098 : 122 -- 144. ISSN 0077 - 8923. PMID 17332070. doi : 10.1196 / annals. 1384.008. Jump up ^ Nater, U.M. ; Rohleder, N. ( 2009 - 05 - 01 ). `` Salivary alpha - amylase as a non-invasive biomarker for the sympathetic nervous system : current state of research ''. Psychoneuroendocrinology. 34 ( 4 ) : 486 -- 496. ISSN 0306 - 4530. PMID 19249160. doi : 10.1016 / j. psyneuen. 2009.01. 014. Jump up ^ `` Falling Number -- Introduction ''. Perten Instruments. 2005. Retrieved 21 November 2009. Jump up ^ `` The use of enzymes in detergents ''. Faculty of Engineering, Science and the Built Environment, London South Bank University. 20 December 2004. Archived from the original on 20 October 2009. Retrieved 21 November 2009. Jump up ^ Fleming, Derek ; Rumbaugh, Kendra P. ( 2017 - 04 - 01 ). `` Approaches to Dispersing Medical Biofilms ''. Microorganisms. 5 ( 2 ). PMID 28368320. doi : 10.3390 / microorganisms5020015. Jump up ^ Fleming, Derek ; Chahin, Laura ; Rumbaugh, Kendra ( February 2017 ). `` Glycoside Hydrolases Degrade Polymicrobial Bacterial Biofilms in Wounds ''. Antimicrobial Agents and Chemotherapy. 61 ( 2 ). ISSN 1098 - 6596. PMC 5278739. PMID 27872074. doi : 10.1128 / AAC. 01998 - 16. Jump up ^ Ghalanbor, Z ; et al. ( 2008 ). `` Binding of Tris to Bacillus licheniformis alpha - amylase can affect its starch hydrolysis activity. ''. Protein Peptide Lett. 15 ( 2 ) : 212 -- 214. PMID 18289113. doi : 10.2174 / 092986608783489616. Jump up ^ Aghajari, N ; et al. ( 1998 ). `` Crystal structures of the psychrophilic alpha - amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. ''. Protein Sci. 7 ( 3 ) : 564 -- 572. PMC 2143949. PMID 9541387. doi : 10.1002 / pro. 5560070304. Jump up ^ Abe A, Yoshida H, Tonozuka T, Sakano Y, Kamitori S ( December 2005 ). `` Complexes of Thermoactinomyces vulgaris R - 47 alpha - amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with alpha - ( 1, 6 ) glycosidic linkages ''. FEBS J. 272 ( 23 ) : 6145 -- 53. PMID 16302977. doi : 10.1111 / j. 1742 - 4658.2005. 05013. x. Jump up ^ Kadziola A, Søgaard M, Svensson B, Haser R ( April 1998 ). `` Molecular structure of a barley alpha - amylase - inhibitor complex : implications for starch binding and catalysis ''. J. Mol. Biol. 278 ( 1 ) : 205 -- 17. PMID 9571044. doi : 10.1006 / jmbi. 1998.1683. Jump up ^ Kadziola A, Abe J, Svensson B, Haser R ( May 1994 ). `` Crystal and molecular structure of barley alpha - amylase ''. J. Mol. Biol. 239 ( 1 ) : 104 -- 21. PMID 8196040. doi : 10.1006 / jmbi. 1994.1354. Jump up ^ Machius M, Wiegand G, Huber R ( March 1995 ). `` Crystal structure of calcium - depleted Bacillus licheniformis alpha - amylase at 2.2 A resolution ''. J. Mol. Biol. 246 ( 4 ) : 545 -- 59. PMID 7877175. doi : 10.1006 / jmbi. 1994.0106. External links The alpha - Amylase Protein alpha - Amylase at the US National Library of Medicine Medical Subject Headings ( MeSH ) This article incorporates text from the public domain Pfam and InterPro IPR006047 This article incorporates text from the public domain Pfam and InterPro IPR012850 This article incorporates text from the public domain Pfam and InterPro IPR006048 Hydrolase : sugar hydrolases ( EC 3.2 ) 3.2. 1 : Glycoside hydrolases Disaccharidase Sucrase / Sucrase - isomaltase / Invertase Maltase Trehalase Lactase Glucosidases Cellulase Alpha - glucosidase Acid Neutral AB Neutral C Beta - glucosidase cytosolic Debranching enzyme Other Amylase Alpha - amylase Chitinase Lysozyme Neuraminidase NEU1 NEU2 NEU3 NEU4 Bacterial neuraminidase Viral neuraminidase Galactosidases Alpha Beta alpha - Mannosidase Glucuronidase Hyaluronidase Pullulanase Glucosylceramidase lysosomal non-lysosomal Galactosylceramidase Alpha - N - acetylgalactosaminidase NAGA Alpha - N - acetylglucosaminidase Fucosidase Hexosaminidase HEXA HEXB Iduronidase Maltase - glucoamylase Heparanase HPSE2 3.2. 2 : Hydrolysing N - Glycosyl compounds DNA glycosylases : Oxoguanine glycosylase Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie -- Hofstee diagram Hanes -- Woolf plot Lineweaver -- Burk plot Michaelis -- Menten kinetics Types EC1 Oxidoreductases ( list ) EC2 Transferases ( list ) EC3 Hydrolases ( list ) EC4 Lyases ( list ) EC5 Isomerases ( list ) EC6 Ligases ( list ) Molecular and Cellular Biology portal Retrieved from `` https://en.wikipedia.org/w/index.php?title=Alpha-amylase&oldid=784975317 '' Categories : EC 3.2. 1 Enzymes Enzymes of known structure Hidden categories : Use dmy dates from June 2013 All articles with unsourced statements Articles with unsourced statements from April 2017 Talk Search Contents About Wikipedia Deutsch Español فارسی Français 한국어 Bahasa Indonesia Íslenska Italiano Lietuvių Magyar Português Српски / srpski Srpskohrvatski / српскохрватски Türkçe Tiếng Việt 中文 Edit links This page was last edited on 10 June 2017, at 23 : 09. 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Question: where is alpha amylase found in the body
Answer: pancreatic juice and saliva,