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Chitinase

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227: 29: 389: 3823: 915: 923: 1065:, and regulation of Ace2p (transcription factor) and cellular morphogenesis (RAM) signalling networks. Overall, the integration of the different regulatory networks allows for the cell wall degrading chitinase to function dependent on the cell's stage in the cell cycle and at specific locations among the daughter cells. 939:
Like cellulose, chitin is an abundant biopolymer that is relatively resistant to degradation. Many mammals can digest chitin and the specific chitinase levels in vertebrate species are adapted to their feeding behaviours. Certain fish are able to digest chitin. Chitinases have been isolated from the
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Regulation varies from species to species, and within an organism, chitinases with different physiological functions would be under different regulation mechanisms. For example, chitinases that are involved in maintenance, such as remodeling the cell wall, are constitutively expressed. However,
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as part of systemic acquired resistance. Expression is mediated by the NPR1 gene and the salicylic acid pathway, both involved in resistance to fungal and insect attack. Other plant chitinases may be required for creating fungal symbioses.
2261:"The chitinase 3-like protein human cartilage glycoprotein 39 (HC-gp39) stimulates proliferation of human connective-tissue cells and activates both extracellular signal-regulated kinase- and protein kinase B-mediated signalling pathways" 986:(worms have chitinous mouthparts to hold the intestinal wall). Finally, the link between chitinases and salicylic acid in plants is well established—but there is a hypothetical link between salicylic acid and allergies in humans. 786:
Chitinases were also classified based on the amino acid sequences, as that would be more helpful in understanding the evolutionary relationships of these enzymes to each other. Therefore, the chitinases were grouped into three
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Waniska RD, Venkatesha RT, Chandrashekar A, Krishnaveni S, Bejosano FP, Jeoung J, et al. (October 2001). "Antifungal proteins and other mechanisms in the control of sorghum stalk rot and grain mold".
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Palmas C, Gabriele F, Conchedda M, Bortoletti G, Ecca AR (June 2003). "Causality or coincidence: may the slow disappearance of helminths be responsible for the imbalances in immune control mechanisms?".
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chitinases had similar characteristics, including the immunological properties, as Class I chitinases. However, Class IV chitinases were significantly smaller in size compared to Class I chitinases.
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And as the gene sequences of the chitinases were known, they were further classified into six classes based on their sequences. Characteristics that determined the classes of chitinases were the
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Although mammals do not produce chitin, they have two functional chitinases, Chitotriosidase (CHIT1) and acidic mammalian chitinase (AMCase), as well as chitinase-like proteins (such as
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and the protein has to localize at the daughter site of the septum. And to do this, there must be coordination with other networks controlling the different phases of the cell, such as
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Chupp GL, Lee CG, Jarjour N, Shim YM, Holm CT, He S, Dziura JD, Reed J, Coyle AJ, Kiener P, Cullen M, Grandsaigne M, Dombret MC, Aubier M, Pretolani M, Elias JA (November 2007).
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Zhu Z, Zheng T, Homer RJ, Kim YK, Chen NY, Cohn L, Hamid Q, Elias JA (June 2004). "Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation".
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Gatehouse AM, Davison GM, Newell CA, Merryweather A, Hamilton WD, Burgess EP, et al. (1997). "Transgenic potato plants with enhanced resistance to the tomato moth,
751:) act on the non-reducing end of the chitin microfibril, releasing the dimer, di-acetylchitobiose, one by one from the chitin chain. Therefore, there is no release of 181: 553:
chitodextrinase, 1,4-β-poly-N-acetylglucosaminidase, poly-β-glucosaminidase, β-1,4-poly-N-acetyl glucosamidinase, poly glycanohydrolase, (1→4)-2-acetamido-2-deoxy-β-
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Chitinases have a wealth of applications, some of which have already been realized by industry. This includes bio-conversion of chitin to useful products such as
873:-terminal but had a similar sequence to Class I chitinases. Class II chitinases were found in plants, fungi, and bacteria and mostly consisted of exochitinases. 425: 263: 200: 3160: 2400:
Zhao J, Zhu H, Wong CH, Leung KY, Wong WS (July 2005). "Increased lungkine and chitinase levels in allergic airway inflammation: a proteomics approach".
2220:"Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family" 911:-terminal seemed to have been lost during evolution, probably due to less selection pressure that caused the catalytic domain to lose its function. 615:), chitinases are generally found in organisms that either need to reshape their own chitin or dissolve and digest the chitin of fungi or animals. 1959: 1537: 1199: 3843: 738:
products. The multimer products includes di-acetylchitobiose, chitotriose, and chitotetraose, with the dimer being the predominant product.
3133: 1975:"Chitin digestibility is dependent on feeding behaviors, which determine acidic chitinase mRNA levels in mammalian and poultry stomachs" 449: 287: 2308:
van Eijk M, van Roomen CP, Renkema GH, Bussink AP, Andrews L, Blommaart EF, Sugar A, Verhoeven AJ, Boot RG, Aerts JM (November 2005).
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Gutowska MA, Drazen JC, Robison BH (November 2004). "Digestive chitinolytic activity in marine fishes of Monterey Bay, California".
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Endochitinases (EC 3.2.1.14) randomly split chitin at internal sites of the chitin microfibril, forming soluble, low molecular mass
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Possible future applications of chitinases are as food additives to increase shelf life, therapeutic agent for asthma and chronic
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or other proteins in rubber latex due to their similar function in plant defense, may trigger an allergic cross-reaction known as
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Elias JA, Homer RJ, Hamid Q, Lee CG (September 2005). "Chitinases and chitinase-like proteins in T(H)2 inflammation and asthma".
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Nelson B, Kurischko C, Horecka J, Mody M, Nair P, Pratt L, Zougman A, McBroom LD, Hughes TR, Boone C, Luca FC (September 2003).
661:, also possess degradative chitinases related to their role as detritivores and also to their potential as arthropod pathogens. 3424: 714: 268: 2744:
Langner T, Göhre V (May 2016). "Fungal chitinases: function, regulation, and potential roles in plant/pathogen interactions".
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Paoletti MG, Norberto L, Damini R, Musumeci S (2007). "Human gastric juice contains chitinase that can degrade chitin".
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chitinases that have specialized functions, such as degrading exogenous chitin or participating in cell division, need
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Muthukrishnan S, Liang GH, Trick HN, Gill BS (2001). "Pathogenesis-related proteins and their genes in cereals".
3693: 2120:"Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins" 990: 154: 3647: 3590: 3173: 3127: 2314: 1029: 767: 745: 706: 679: 545: 59: 2934:"RAM: a conserved signaling network that regulates Ace2p transcriptional activity and polarized morphogenesis" 849:
localization. And then, Class I chitinases were further subdivided based on their acidic or basic nature into
773:) split the multimer products, such as di-acetylchitobiose, chitotriose, and chitotetraose, into monomers of 141: 3595: 3346: 1431: 861:, respectively. Class 1 chitinases were found to comprise only plant chitinases and mostly endochitinases. 3509: 3254: 2039: 1637:"Potential role of chitinase 3-like-1 in inflammation-associated carcinogenic changes of epithelial cells" 1215:
Sámi L, Pusztahelyi T, Emri T, Varecza Z, Fekete A, Grallert A, Karanyi Z, Kiss L, Pócsi I (August 2001).
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Bierbaum S, Nickel R, Koch A, Lau S, Deichmann KA, Wahn U, Superti-Furga A, Heinzmann A (December 2005).
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acetylglucosamine, which would be possibly taken up and triggers up-regulation of the chitinbiosidases.
129: 3688: 709:. Ignatius et al also find these (seed and leaf isozymes) to differ from each other. Some of these are 2570:
Maizels RM (December 2005). "Infections and allergy - helminths, hygiene and host immune regulation".
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acetylglucosaminidase, and the data indicates a feedback-loop where the break down of chitin produces
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chitinases are not well characterized. However, one example of a Class V chitinase showed two chitin
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Salzer P, Bonanomi A, Beyer K, Vögeli-Lange R, Aeschbacher RA, Lange J, et al. (July 2000).
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Tabata E, Kashimura A, Kikuchi A, Masuda H, Miyahara R, Hiruma Y, et al. (January 2018).
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Brunner K, Peterbauer CK, Mach RL, Lorito M, Zeilinger S, Kubicek CP (July 2003). "The Nag1
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cultures under carbon starvation: Chitinase production and antifungal effect of allosamidin"
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Chitinases production in the human body (known as "human chitinases") may be in response to
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Patil RS, Ghormade V, Deshpande MV (April 2000). "Chitinolytic enzymes: an exploration".
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Exochitinase breaking down chitin into dimers via chitobiosidase and monomers via β-1,4-
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Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology
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Basra, A.S. (2007). "3. Seed Ecology Chapter 16. Natural defense mechanisms in seeds".
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is essential for chitinase induction by chitin and of major relevance to biocontrol".
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Akaki C, Duke GE (2005). "Apparent chitin digestibilities in the Eastern screech owl (
1787: 3837: 3621: 3580: 3392: 3321: 3304: 3123: 2623: 2606: 2531:"A chitinase-like protein in the lung and circulation of patients with severe asthma" 2186: 1464: 1285: 1111: 1107: 1091: 1046: 624: 3023: 2824: 2773: 2727: 2684: 2640: 2515: 2429: 2104: 1897:
Collinge DB, Kragh KM, Mikkelsen JD, Nielsen KK, Rasmussen U, Vad K (January 1993).
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Hamid R, Khan MA, Ahmad M, Ahmad MM, Abdin MZ, Musarrat J, Javed S (January 2013).
1811:"A classification of glycosyl hydrolases based on amino acid sequence similarities" 1062: 656: 3134:
The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis
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Human chitinases may explain the link between some of the most common allergies (
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10.1002/(SICI)1097-010X(19990301/01)283:4/5<387::AID-JEZ8>3.0.CO;2-W
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Flach J, Pilet PE, Jollès P (August 1992). "What's new in chitinase research?".
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chitinases did not have similar sequences to chitinases in Class I or Class II.
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Renkema GH, Boot RG, Muijsers AO, Donker-Koopman WE, Aerts JM (February 1995).
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May be used to monitor enzymotherapy supplementation in Gaucher's disease.
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roots during mycorrhiza formation, nodulation, and pathogen infection"
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Gomez L, Allona I, Casado R, Aragoncillo C (2002). "Seed chitinases".
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chitinase 1), one of the chitinases involved in cell separation after
951:. As in plant chitinases this may be related to pathogen resistance. 674: 402: 240: 44: 3781: 3551: 1529: 964: 722: 665: 635: 576: 568: 461: 299: 188: 100: 88: 76: 1319:"Conservation of the chitin utilization pathway in the Vibrionaceae" 1260:
Xiao X, Yin X, Lin J, Sun L, You Z, Wang P, Wang F (December 2005).
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with these qualities are already being produced) and enhancement of
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Some parts of chitinase molecules, almost identical in structure to
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acidic mammalian chitinase with bound inhibitor methylallosamidin.
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chitotriosidase bound with two molecules of inhibitor allosamidin
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Feingold BF (March 1975). "Food additives in clinical medicine".
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Eurich K, Segawa M, Toei-Shimizu S, Mizoguchi E (November 2009).
3456: 3451: 3412: 3341: 3336: 3331: 3326: 3276: 3264: 1262:"Chitinase genes in lake sediments of Ardley Island, Antarctica" 975: 454: 292: 112: 3524: 3142: 1049:, there must be tight regulation and activation. Specifically, 705:). Ignatius et al 1994(b) find these in the leaves, induced by 741:
Exochitinases have also been divided into two sub categories:
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expression has to be activated in daughter cells during late
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in tandem, and based on the gene sequence, the cysteine-rich
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or fungi or they may degrade the remains of these organisms.
2840:"Chitinase is required for cell separation during growth of 591:-glucosaminide (1→4)-β-linkages in chitin and chitodextrins 3520: 2357:
American Journal of Respiratory and Critical Care Medicine
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Endochitinase breaking down chitin into multimer products.
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has been linked to enhanced chitinase expression levels.
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Hunt DE, Gevers D, Vahora NM, Polz MF (January 2008).
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gas, may stimulate increased production of chitinase.
3811: 1734:: Purification of Chitobiosidase and Endochitinase". 1592:"Differential expression of eight chitinase genes in 664:
Chitinases are also present in plants – for example
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chitinase A dimer with bound inhibitor allosamidin.
3707: 3671: 3640: 3609: 3558: 3493: 3292: 3235: 3194: 3181: 2883:Colman-Lerner A, Chin TE, Brent R (December 2001). 525: 515: 510: 489: 484: 472: 460: 448: 436: 424: 416: 411: 381: 363: 353: 348: 327: 322: 310: 298: 286: 274: 262: 254: 249: 219: 199: 187: 175: 170: 147: 135: 123: 111: 99: 87: 75: 70: 58: 53: 21: 2171:"Chitinase activity in human serum and leukocytes" 1424: 1422: 2218:Hakala BE, White C, Recklies AD (December 1993). 1073:Chitinases occur naturally in many common foods. 943:Chitinase activity can also be detected in human 689:in Ignatius et al 1994(a). They find clone 10, a 1045:. As these types of chitinases are important in 974:, mold spores—both of which contain chitin) and 821:-terminal sequence, localization of the enzyme, 3038:"Latex-Fruit Syndrome and Class 2 Food Allergy" 1225:The Journal of General and Applied Microbiology 1106:, the production of non-allergenic, non-toxic, 623:Chitinivorous organisms include many bacteria ( 2445:The Journal of Allergy and Clinical Immunology 3536: 3154: 1769: 1767: 1765: 1763: 1761: 1759: 1757: 8: 3075:Journal of Pharmacy & Bioallied Sciences 982:) infections, as part of one version of the 807:acetylglucosaminidase and a similar enzyme, 1730:Harman GE (1993). "Chitinolytic Enzymes of 697:during development. 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Barley seeds are found to produce 607:elements of some animals (including 2848:The Journal of Biological Chemistry 2535:The New England Journal of Medicine 2224:The Journal of Biological Chemistry 2124:The Journal of Biological Chemistry 1689:Sahai AS, Manocha MS (1993-08-01). 1059:Cdc14 Early Anaphase Release (FEAR) 3042:Division of Medical Devices, Japan 2712:10.1111/j.1365-4362.1975.tb01426.x 1708:10.1111/j.1574-6976.1993.tb00004.x 711:pathogenesis related (PR) proteins 14: 1641:World Journal of Gastroenterology 3821: 2624:10.1111/j.0269-2813.2004.01803.x 2187:10.1128/IAI.63.12.4770-4773.1995 1286:10.1128/AEM.71.12.7904-7909.2005 1190:Jollès P, Muzzarelli RA (1999). 595:As chitin is a component of the 3425:Alpha-N-acetylgalactosaminidase 1948:Journal of Experimental Zoology 1776:Enzyme and Microbial Technology 1150:into entirely unrelated crops. 1041:by degrading the chitin of the 1033:and the regulation of ScCts1p ( 841:chitinases had a cysteine-rich 639:, among others), which may be 1: 3437:Alpha-N-acetylglucosaminidase 2938:Molecular Biology of the Cell 2902:10.1016/S0092-8674(01)00596-7 2861:10.1016/S0021-9258(18)55057-2 2572:Current Opinion in Immunology 2237:10.1016/S0021-9258(19)74461-5 1809:Henrissat B (December 1991). 1788:10.1016/s0141-0229(00)00134-4 382:chitinase 1 (chitotriosidase) 1942:) and the American kestrel ( 561:(1→4)-2-acetamido-2-deoxy-β- 3844:Genes on human chromosome 1 1817:. 280 ( Pt 2) (2): 309–16. 1004:of the chitinase activity. 3870: 2791:-acetylglucosaminidase of 2457:10.1016/j.jaci.2005.06.028 2054:10.1016/j.cbpb.2004.09.020 1999:10.1038/s41598-018-19940-8 1613:10.1094/MPMI.2000.13.7.763 1441:Cambridge University Press 1063:mitotic exit network (MEN) 1002:spatio-temporal regulation 583:Random endo-hydrolysis of 3699:Michaelis–Menten kinetics 3000:Springer Science+Business 2809:10.1007/s00294-003-0399-y 2758:10.1007/s00294-015-0530-x 2584:10.1016/j.coi.2005.09.001 2369:10.1164/rccm.200506-890OC 1695:FEMS Microbiology Reviews 1489:American Chemical Society 766:-acetylglucosaminidases ( 506: 386: 344: 224: 166: 26: 3591:Diffusion-limited enzyme 3128:Medical Subject Headings 3088:10.4103/0975-7406.106559 2842:Saccharomyces cerevisiae 2657:Journal of Helminthology 2315:International Immunology 1217:"Autolysis and aging of 1030:Saccharomyces cerevisiae 565:-glucan glycanohydrolase 557:-glucan glycanohydrolase 3347:Bacterial neuraminidase 3071:"Chitinases: An update" 3008:10.1023/a:1009600321838 2988:: growth room trials". 2950:10.1091/mbc.E03-01-0018 2500:10.1126/science.1095336 2265:The Biochemical Journal 1815:The Biochemical Journal 1397:10.1023/a:1010763506802 1219:Penicillium chrysogenum 930:-acetylglucosaminidase. 701:(as well as several of 3510:Oxoguanine glycosylase 2793:Trichoderma atroviride 2414:10.1002/pmic.200401169 2175:Infection and Immunity 2137:10.1074/jbc.270.5.2198 931: 919: 3684:Eadie–Hofstee diagram 3617:Allosteric regulation 2329:10.1093/intimm/dxh328 1732:Trichoderma harzianum 1432:Seed Science Research 1194:. Basel: Birkhäuser. 1192:Chitin and Chitinases 955:Clinical significance 925: 917: 812:-acetylhexosaminidase 3694:Lineweaver–Burk plot 3499:N-Glycosyl compounds 3469:Maltase-glucoamylase 3420:Galactosylceramidase 3187:Glycoside hydrolases 3172:: sugar hydrolases ( 2548:10.1056/NEJMoa073600 1748:10.1094/phyto-83-313 1343:10.1128/AEM.01412-07 1092:latex-fruit syndrome 619:Species distribution 3352:Viral neuraminidase 2492:2004Sci...304.1678Z 1991:2018NatSR...8.1461T 1654:10.3748/wjg.15.5249 1594:Medicago truncatula 1335:2008ApEnM..74...44H 1278:2005ApEnM..71.7904X 1238:10.2323/jgam.47.201 1159:protein engineering 995:Regulation in fungi 778:-acetylglucoseamine 35:Serratia marcescens 3653:Enzyme superfamily 3586:Enzyme promiscuity 3403:Glucosylceramidase 3284:Debranching enzyme 3208:Sucrase-isomaltase 2991:Molecular Breeding 2986:Lacanobia oleracea 2669:10.1079/JOH2003176 2277:10.1042/BJ20020075 1979:Scientific Reports 1899:"Plant chitinases" 1868:10.1007/BF02124285 1491:(ACS): 4732–4742. 1449:10.1079/ssr2002113 1136:Phaseolus vulgaris 1076:Phaseolus vulgaris 1016:is dependent on a 984:hygiene hypothesis 932: 920: 559:; systematic name 3809: 3808: 3518: 3517: 3489: 3488: 3376:alpha-Mannosidase 3250:Alpha-glucosidase 2486:(5677): 1678–82. 2089:10.1159/000104144 1903:The Plant Journal 1823:10.1042/bj2800309 1539:978-93-88148-36-8 1497:10.1021/jf010007f 1201:978-3-7643-5815-0 1142:, BCH - has been 759:in this reaction. 744:Chitobiosidases ( 691:Class I chitinase 590: 567:) are hydrolytic 564: 556: 539: 538: 535: 534: 377: 376: 373: 372: 220:chitinase, acidic 215: 214: 211: 210: 130:metabolic pathway 3861: 3826: 3825: 3817: 3689:Hanes–Woolf plot 3632:Enzyme activator 3627:Enzyme inhibitor 3601:Enzyme catalysis 3545: 3538: 3531: 3522: 3506:DNA glycosylases 3272:Beta-glucosidase 3192: 3163: 3156: 3149: 3140: 3111: 3110: 3100: 3090: 3066: 3057: 3056: 3054: 3053: 3044:. Archived from 3034: 3028: 3027: 2981: 2972: 2971: 2961: 2929: 2923: 2922: 2904: 2880: 2874: 2873: 2863: 2854:(29): 19758–67. 2835: 2829: 2828: 2797:Current Genetics 2784: 2778: 2777: 2746:Current Genetics 2741: 2732: 2731: 2695: 2689: 2688: 2651: 2645: 2644: 2626: 2602: 2596: 2595: 2567: 2561: 2560: 2550: 2526: 2520: 2519: 2475: 2469: 2468: 2440: 2434: 2433: 2408:(11): 2799–807. 2397: 2391: 2390: 2380: 2348: 2342: 2341: 2331: 2305: 2299: 2298: 2288: 2271:(Pt 1): 119–26. 2256: 2250: 2249: 2239: 2230:(34): 25803–10. 2215: 2209: 2208: 2198: 2166: 2160: 2159: 2149: 2139: 2115: 2109: 2108: 2072: 2066: 2065: 2047: 2027: 2021: 2020: 2010: 1970: 1964: 1963: 1954:(4–5): 387–393. 1944:Falco sparverius 1935: 1929: 1928: 1918: 1894: 1888: 1887: 1851: 1845: 1844: 1834: 1806: 1800: 1799: 1771: 1752: 1751: 1727: 1721: 1720: 1710: 1686: 1677: 1676: 1666: 1656: 1632: 1626: 1625: 1615: 1587: 1581: 1565: 1563: 1562: 1530:10.2307/25065722 1515: 1509: 1508: 1475: 1469: 1468: 1443:(CUP): 217–230. 1426: 1417: 1416: 1374: 1365: 1364: 1354: 1314: 1308: 1307: 1297: 1257: 1251: 1250: 1240: 1212: 1206: 1205: 1187: 1069:Presence in food 902: 901: 896: 895: 888: 887: 880: 879: 868: 867: 860: 859: 854: 853: 840: 839: 757:oligosaccharides 677: 668:seed chitinase: 588: 573:glycosidic bonds 571:that break down 562: 554: 508: 405: 391: 379: 346: 243: 229: 217: 168: 47: 31: 19: 3869: 3868: 3864: 3863: 3862: 3860: 3859: 3858: 3834: 3833: 3832: 3820: 3812: 3810: 3805: 3717:Oxidoreductases 3703: 3679:Enzyme kinetics 3667: 3663:List of enzymes 3636: 3605: 3576:Catalytic triad 3554: 3549: 3519: 3514: 3498: 3485: 3288: 3231: 3177: 3167: 3120: 3115: 3114: 3068: 3067: 3060: 3051: 3049: 3036: 3035: 3031: 2983: 2982: 2975: 2944:(9): 3782–803. 2931: 2930: 2926: 2882: 2881: 2877: 2837: 2836: 2832: 2786: 2785: 2781: 2743: 2742: 2735: 2697: 2696: 2692: 2653: 2652: 2648: 2604: 2603: 2599: 2569: 2568: 2564: 2541:(20): 2016–27. 2528: 2527: 2523: 2477: 2476: 2472: 2442: 2441: 2437: 2399: 2398: 2394: 2350: 2349: 2345: 2322:(11): 1505–12. 2307: 2306: 2302: 2258: 2257: 2253: 2217: 2216: 2212: 2168: 2167: 2163: 2130:(5): 2198–202. 2117: 2116: 2112: 2074: 2073: 2069: 2045:10.1.1.318.6544 2029: 2028: 2024: 1972: 1971: 1967: 1937: 1936: 1932: 1896: 1895: 1891: 1853: 1852: 1848: 1808: 1807: 1803: 1773: 1772: 1755: 1729: 1728: 1724: 1688: 1687: 1680: 1647:(42): 5249–59. 1634: 1633: 1629: 1589: 1588: 1584: 1560: 1558: 1540: 1517: 1516: 1512: 1477: 1476: 1472: 1428: 1427: 1420: 1389:Kluwer Academic 1376: 1375: 1368: 1316: 1315: 1311: 1259: 1258: 1254: 1214: 1213: 1209: 1202: 1189: 1188: 1184: 1179: 1167: 1120:artificial skin 1100: 1071: 997: 957: 937: 905:binding domains 899: 898: 893: 892: 885: 884: 877: 876: 865: 864: 857: 856: 851: 850: 837: 836: 753:monosaccharides 731: 703:β-1,3-glucanase 669: 654:Fungi, such as 621: 407: 397: 245: 235: 49: 39: 17: 12: 11: 5: 3867: 3865: 3857: 3856: 3851: 3846: 3836: 3835: 3831: 3830: 3807: 3806: 3804: 3803: 3790: 3777: 3764: 3751: 3738: 3725: 3711: 3709: 3705: 3704: 3702: 3701: 3696: 3691: 3686: 3681: 3675: 3673: 3669: 3668: 3666: 3665: 3660: 3655: 3650: 3644: 3642: 3641:Classification 3638: 3637: 3635: 3634: 3629: 3624: 3619: 3613: 3611: 3607: 3606: 3604: 3603: 3598: 3593: 3588: 3583: 3578: 3573: 3568: 3562: 3560: 3556: 3555: 3550: 3548: 3547: 3540: 3533: 3525: 3516: 3515: 3513: 3512: 3502: 3500: 3491: 3490: 3487: 3486: 3484: 3483: 3482: 3481: 3471: 3466: 3461: 3460: 3459: 3454: 3447:Hexosaminidase 3444: 3439: 3434: 3433: 3432: 3422: 3417: 3416: 3415: 3410: 3400: 3395: 3390: 3389: 3388: 3378: 3373: 3372: 3371: 3366: 3359:Galactosidases 3356: 3355: 3354: 3349: 3344: 3339: 3334: 3329: 3319: 3314: 3309: 3308: 3307: 3296: 3294: 3290: 3289: 3287: 3286: 3281: 3280: 3279: 3269: 3268: 3267: 3262: 3257: 3247: 3241: 3239: 3233: 3232: 3230: 3229: 3224: 3219: 3214: 3200: 3198: 3196:Disaccharidase 3189: 3179: 3178: 3168: 3166: 3165: 3158: 3151: 3143: 3137: 3136: 3131: 3119: 3118:External links 3116: 3113: 3112: 3058: 3029: 2973: 2924: 2875: 2830: 2779: 2733: 2690: 2646: 2597: 2562: 2521: 2470: 2451:(3): 497–500. 2435: 2392: 2363:(12): 1505–9. 2343: 2300: 2251: 2210: 2181:(12): 4770–3. 2161: 2110: 2067: 2022: 1965: 1930: 1889: 1862:(8): 701–716. 1846: 1801: 1782:(7): 473–483. 1753: 1736:Phytopathology 1722: 1701:(4): 317–338. 1678: 1627: 1606:(7): 763–777. 1582: 1538: 1510: 1470: 1418: 1366: 1309: 1272:(12): 7904–9. 1252: 1231:(4): 201–211. 1207: 1200: 1181: 1180: 1178: 1175: 1174: 1173: 1166: 1163: 1155:rhinosinusitis 1148:pest deterrent 1146:inserted as a 1144:transgenically 1140:bean chitinase 1116:contact lenses 1099: 1096: 1070: 1067: 1043:primary septum 996: 993: 956: 953: 936: 933: 827:signal peptide 823:isoelectric pH 784: 783: 782: 781: 760: 739: 730: 729:Classification 727: 707:powdery mildew 693:, in the seed 620: 617: 593: 592: 537: 536: 533: 532: 527: 523: 522: 517: 513: 512: 504: 503: 493: 487: 486: 482: 481: 476: 470: 469: 464: 458: 457: 452: 446: 445: 440: 434: 433: 428: 422: 421: 418: 414: 413: 409: 408: 392: 384: 383: 375: 374: 371: 370: 365: 361: 360: 355: 351: 350: 342: 341: 331: 325: 324: 320: 319: 314: 308: 307: 302: 296: 295: 290: 284: 283: 278: 272: 271: 266: 260: 259: 256: 252: 251: 247: 246: 230: 222: 221: 213: 212: 209: 208: 203: 197: 196: 191: 185: 184: 179: 173: 172: 164: 163: 152: 145: 144: 139: 133: 132: 127: 121: 120: 115: 109: 108: 103: 97: 96: 91: 85: 84: 79: 73: 72: 68: 67: 62: 56: 55: 51: 50: 32: 24: 23: 15: 13: 10: 9: 6: 4: 3: 2: 3866: 3855: 3852: 3850: 3847: 3845: 3842: 3841: 3839: 3829: 3824: 3819: 3815: 3801: 3797: 3796: 3791: 3788: 3784: 3783: 3778: 3775: 3771: 3770: 3765: 3762: 3758: 3757: 3752: 3749: 3745: 3744: 3739: 3736: 3732: 3731: 3726: 3723: 3719: 3718: 3713: 3712: 3710: 3706: 3700: 3697: 3695: 3692: 3690: 3687: 3685: 3682: 3680: 3677: 3676: 3674: 3670: 3664: 3661: 3659: 3658:Enzyme family 3656: 3654: 3651: 3649: 3646: 3645: 3643: 3639: 3633: 3630: 3628: 3625: 3623: 3622:Cooperativity 3620: 3618: 3615: 3614: 3612: 3608: 3602: 3599: 3597: 3594: 3592: 3589: 3587: 3584: 3582: 3581:Oxyanion hole 3579: 3577: 3574: 3572: 3569: 3567: 3564: 3563: 3561: 3557: 3553: 3546: 3541: 3539: 3534: 3532: 3527: 3526: 3523: 3511: 3507: 3504: 3503: 3501: 3497:: Hydrolysing 3496: 3492: 3480: 3477: 3476: 3475: 3472: 3470: 3467: 3465: 3462: 3458: 3455: 3453: 3450: 3449: 3448: 3445: 3443: 3440: 3438: 3435: 3431: 3428: 3427: 3426: 3423: 3421: 3418: 3414: 3413:non-lysosomal 3411: 3409: 3406: 3405: 3404: 3401: 3399: 3396: 3394: 3393:Hyaluronidase 3391: 3387: 3384: 3383: 3382: 3381:Glucuronidase 3379: 3377: 3374: 3370: 3367: 3365: 3362: 3361: 3360: 3357: 3353: 3350: 3348: 3345: 3343: 3340: 3338: 3335: 3333: 3330: 3328: 3325: 3324: 3323: 3322:Neuraminidase 3320: 3318: 3315: 3313: 3310: 3306: 3305:Alpha-amylase 3303: 3302: 3301: 3298: 3297: 3295: 3291: 3285: 3282: 3278: 3275: 3274: 3273: 3270: 3266: 3263: 3261: 3258: 3256: 3253: 3252: 3251: 3248: 3246: 3243: 3242: 3240: 3238: 3234: 3228: 3225: 3223: 3220: 3218: 3215: 3213: 3209: 3205: 3202: 3201: 3199: 3197: 3193: 3190: 3188: 3184: 3180: 3175: 3171: 3164: 3159: 3157: 3152: 3150: 3145: 3144: 3141: 3135: 3132: 3129: 3125: 3122: 3121: 3117: 3108: 3104: 3099: 3094: 3089: 3084: 3080: 3076: 3072: 3065: 3063: 3059: 3048:on 2020-11-11 3047: 3043: 3039: 3033: 3030: 3025: 3021: 3017: 3013: 3009: 3005: 3001: 2997: 2993: 2992: 2987: 2980: 2978: 2974: 2969: 2965: 2960: 2955: 2951: 2947: 2943: 2939: 2935: 2928: 2925: 2920: 2916: 2912: 2908: 2903: 2898: 2895:(6): 739–50. 2894: 2890: 2886: 2879: 2876: 2871: 2867: 2862: 2857: 2853: 2849: 2845: 2843: 2834: 2831: 2826: 2822: 2818: 2814: 2810: 2806: 2803:(4): 289–95. 2802: 2798: 2794: 2790: 2783: 2780: 2775: 2771: 2767: 2763: 2759: 2755: 2752:(2): 243–54. 2751: 2747: 2740: 2738: 2734: 2729: 2725: 2721: 2717: 2713: 2709: 2705: 2701: 2694: 2691: 2686: 2682: 2678: 2674: 2670: 2666: 2663:(2): 147–53. 2662: 2658: 2650: 2647: 2642: 2638: 2634: 2630: 2625: 2620: 2617:(2): 167–77. 2616: 2612: 2608: 2601: 2598: 2593: 2589: 2585: 2581: 2578:(6): 656–61. 2577: 2573: 2566: 2563: 2558: 2554: 2549: 2544: 2540: 2536: 2532: 2525: 2522: 2517: 2513: 2509: 2505: 2501: 2497: 2493: 2489: 2485: 2481: 2474: 2471: 2466: 2462: 2458: 2454: 2450: 2446: 2439: 2436: 2431: 2427: 2423: 2419: 2415: 2411: 2407: 2403: 2396: 2393: 2388: 2384: 2379: 2374: 2370: 2366: 2362: 2358: 2354: 2347: 2344: 2339: 2335: 2330: 2325: 2321: 2317: 2316: 2311: 2304: 2301: 2296: 2292: 2287: 2282: 2278: 2274: 2270: 2266: 2262: 2255: 2252: 2247: 2243: 2238: 2233: 2229: 2225: 2221: 2214: 2211: 2206: 2202: 2197: 2192: 2188: 2184: 2180: 2176: 2172: 2165: 2162: 2157: 2153: 2148: 2143: 2138: 2133: 2129: 2125: 2121: 2114: 2111: 2106: 2102: 2098: 2094: 2090: 2086: 2083:(3): 244–51. 2082: 2078: 2071: 2068: 2063: 2059: 2055: 2051: 2046: 2041: 2037: 2033: 2026: 2023: 2018: 2014: 2009: 2004: 2000: 1996: 1992: 1988: 1984: 1980: 1976: 1969: 1966: 1961: 1957: 1953: 1949: 1945: 1941: 1934: 1931: 1926: 1922: 1917: 1912: 1908: 1904: 1900: 1893: 1890: 1885: 1881: 1877: 1873: 1869: 1865: 1861: 1857: 1850: 1847: 1842: 1838: 1833: 1828: 1824: 1820: 1816: 1812: 1805: 1802: 1797: 1793: 1789: 1785: 1781: 1777: 1770: 1768: 1766: 1764: 1762: 1760: 1758: 1754: 1749: 1745: 1741: 1737: 1733: 1726: 1723: 1718: 1714: 1709: 1704: 1700: 1696: 1692: 1685: 1683: 1679: 1674: 1670: 1665: 1660: 1655: 1650: 1646: 1642: 1638: 1631: 1628: 1623: 1619: 1614: 1609: 1605: 1601: 1597: 1595: 1586: 1583: 1579: 1575: 1572: 1571:9788172335731 1568: 1557: 1553: 1549: 1545: 1541: 1535: 1531: 1527: 1523: 1522: 1514: 1511: 1506: 1502: 1498: 1494: 1490: 1486: 1482: 1474: 1471: 1466: 1462: 1458: 1454: 1450: 1446: 1442: 1438: 1434: 1433: 1425: 1423: 1419: 1414: 1410: 1406: 1402: 1398: 1394: 1390: 1386: 1382: 1381: 1373: 1371: 1367: 1362: 1358: 1353: 1348: 1344: 1340: 1336: 1332: 1328: 1324: 1320: 1313: 1310: 1305: 1301: 1296: 1291: 1287: 1283: 1279: 1275: 1271: 1267: 1263: 1256: 1253: 1248: 1244: 1239: 1234: 1230: 1226: 1222: 1220: 1211: 1208: 1203: 1197: 1193: 1186: 1183: 1176: 1172: 1169: 1168: 1164: 1162: 1160: 1156: 1151: 1149: 1145: 1141: 1137: 1133: 1129: 1125: 1121: 1117: 1113: 1112:biodegradable 1109: 1108:biocompatible 1105: 1097: 1095: 1093: 1089: 1084: 1082: 1078: 1077: 1068: 1066: 1064: 1060: 1056: 1052: 1048: 1047:cell division 1044: 1040: 1036: 1035:S. cerevisiae 1032: 1031: 1025: 1023: 1019: 1015: 1014: 1011: 1005: 1003: 994: 992: 991: 987: 985: 981: 977: 973: 968: 966: 962: 954: 952: 950: 947:and possibly 946: 941: 934: 929: 924: 916: 912: 910: 906: 890: 882: 874: 872: 862: 848: 844: 834: 832: 828: 824: 820: 815: 813: 811: 806: 802: 798: 794: 790: 779: 777: 772: 769: 765: 761: 758: 754: 750: 747: 743: 742: 740: 737: 733: 732: 728: 726: 724: 719: 716: 712: 708: 704: 700: 696: 692: 688: 684: 681: 676: 672: 667: 662: 660: 658: 652: 650: 646: 642: 638: 637: 632: 631: 626: 618: 616: 614: 610: 606: 602: 598: 586: 582: 581: 580: 578: 574: 570: 566: 558: 550: 547: 543: 531: 528: 524: 521: 518: 514: 509: 505: 502: 501: 497: 494: 492: 488: 483: 480: 477: 475: 471: 468: 465: 463: 459: 456: 453: 451: 447: 444: 441: 439: 435: 432: 429: 427: 423: 419: 415: 410: 404: 400: 395: 390: 385: 380: 369: 366: 362: 359: 356: 352: 347: 343: 340: 339: 335: 332: 330: 326: 321: 318: 315: 313: 309: 306: 303: 301: 297: 294: 291: 289: 285: 282: 279: 277: 273: 270: 267: 265: 261: 257: 253: 248: 242: 238: 233: 228: 223: 218: 207: 204: 202: 198: 195: 192: 190: 186: 183: 180: 178: 174: 169: 165: 162: 159: 156: 153: 150: 146: 143: 140: 138: 134: 131: 128: 126: 122: 119: 116: 114: 110: 107: 106:NiceZyme view 104: 102: 98: 95: 92: 90: 86: 83: 80: 78: 74: 69: 66: 63: 61: 57: 52: 46: 42: 37: 36: 30: 25: 20: 3795:Translocases 3792: 3779: 3766: 3753: 3740: 3730:Transferases 3727: 3714: 3571:Binding site 3311: 3237:Glucosidases 3078: 3074: 3050:. Retrieved 3046:the original 3041: 3032: 2995: 2989: 2985: 2941: 2937: 2927: 2892: 2888: 2878: 2851: 2847: 2841: 2833: 2800: 2796: 2792: 2788: 2782: 2749: 2745: 2706:(2): 112–4. 2703: 2699: 2693: 2660: 2656: 2649: 2614: 2610: 2600: 2575: 2571: 2565: 2538: 2534: 2524: 2483: 2479: 2473: 2448: 2444: 2438: 2405: 2401: 2395: 2360: 2356: 2346: 2319: 2313: 2303: 2268: 2264: 2254: 2227: 2223: 2213: 2178: 2174: 2164: 2127: 2123: 2113: 2080: 2076: 2070: 2038:(3): 351–8. 2035: 2031: 2025: 1982: 1978: 1968: 1951: 1947: 1943: 1939: 1933: 1909:(1): 31–40. 1906: 1902: 1892: 1859: 1855: 1849: 1814: 1804: 1779: 1775: 1739: 1735: 1731: 1725: 1698: 1694: 1644: 1640: 1630: 1603: 1599: 1593: 1585: 1559:. Retrieved 1520: 1513: 1484: 1480: 1473: 1436: 1430: 1384: 1378: 1329:(1): 44–51. 1326: 1322: 1312: 1269: 1265: 1255: 1228: 1224: 1218: 1210: 1191: 1185: 1152: 1138:chitinase - 1135: 1128:insecticides 1101: 1098:Applications 1085: 1074: 1072: 1050: 1034: 1028: 1026: 1021: 1017: 1008: 1006: 998: 988: 969: 958: 942: 938: 927: 908: 891: 883: 875: 870: 863: 842: 835: 818: 816: 809: 804: 785: 775: 763: 720: 663: 657:Coccidioides 655: 653: 634: 628: 622: 594: 584: 560: 552: 541: 540: 498: 394:Homo sapiens 393: 336: 305:NM_001040623 232:Homo sapiens 231: 94:BRENDA entry 33: 3566:Active site 3464:Iduronidase 3398:Pullulanase 3081:(1): 21–9. 1985:(1): 1461. 1856:Experientia 1114:materials ( 1039:cytokinesis 1010:Trichoderma 649:zooplankton 605:exoskeletal 520:Swiss-model 412:Identifiers 358:Swiss-model 250:Identifiers 82:IntEnz view 54:Identifiers 3838:Categories 3769:Isomerases 3743:Hydrolases 3610:Regulation 3474:Heparanase 3442:Fucosidase 3260:Neutral AB 3052:2017-02-16 2402:Proteomics 2147:1887/50684 1742:(3): 313. 1578:9388148363 1561:2021-11-17 1391:: 93–114. 1177:References 1132:fungicides 1104:fertilizer 1013:atroviride 972:dust mites 645:arthropods 641:pathogenic 625:Aeromonads 613:arthropods 597:cell walls 587:-acetyl-β- 542:Chitinases 516:Structures 511:Search for 485:Other data 354:Structures 349:Search for 338:p13.1-21.3 323:Other data 151:structures 118:KEGG entry 3648:EC number 3408:lysosomal 3312:Chitinase 3277:cytosolic 3265:Neutral C 3245:Cellulase 3222:Trehalase 3212:Invertase 3170:Hydrolase 3124:Chitinase 3016:1380-3743 3002:: 49–63. 2040:CiteSeerX 1940:Otus asio 1465:233361411 1457:0960-2585 1405:0167-6857 1171:Ligninase 961:allergies 949:cartilage 878:Class III 780:(GlcNAc). 713:that are 678:​, 467:NM_003465 426:NCBI gene 264:NCBI gene 71:Databases 22:Chitinase 3849:EC 3.2.1 3672:Kinetics 3596:Cofactor 3559:Activity 3317:Lysozyme 3107:23559820 3024:23765916 2968:12972564 2911:11747810 2825:22135834 2817:12748812 2774:10360301 2766:26527115 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965:asthma 963:, and 829:, and 799:, and 723:YKL-40 666:barley 636:Vibrio 577:chitin 496:Chr. 1 479:Q13231 462:RefSeq 455:600031 417:Symbol 334:Chr. 1 317:Q9BZP6 300:RefSeq 293:606080 255:Symbol 189:PubMed 171:Search 161:PDBsum 101:ExPASy 89:BRENDA 77:IntEnz 60:EC no. 3708:Types 3495:3.2.2 3479:HPSE2 3364:Alpha 3293:Other 3183:3.2.1 3020:S2CID 2998:(1). 2915:S2CID 2821:S2CID 2770:S2CID 2724:S2CID 2681:S2CID 2637:S2CID 2512:S2CID 2426:S2CID 2101:S2CID 1880:S2CID 1713:S2CID 1552:S2CID 1544:JSTOR 1461:S2CID 1439:(4). 1409:S2CID 945:blood 601:fungi 491:Locus 420:CHIT1 329:Locus 281:17432 269:27159 137:PRIAM 3800:list 3793:EC7 3787:list 3780:EC6 3774:list 3767:EC5 3761:list 3754:EC4 3748:list 3741:EC3 3735:list 3728:EC2 3722:list 3715:EC1 3457:HEXB 3452:HEXA 3430:NAGA 3369:Beta 3342:NEU4 3337:NEU3 3332:NEU2 3327:NEU1 3255:Acid 3176:3.2) 3103:PMID 3012:ISSN 2964:PMID 2907:PMID 2889:Cell 2866:PMID 2813:PMID 2762:PMID 2716:PMID 2673:PMID 2629:PMID 2588:PMID 2553:PMID 2504:PMID 2461:PMID 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Index


Serratia marcescens
PDB
1FFQ
EC no.
3.2.1.14
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB
RCSB PDB
PDBe
PDBsum
PMC
articles
PubMed
articles
NCBI
proteins

PDB

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