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{{enzyme
{{enzyme
| Name = Chitinase
| Name = Chitinase
| EC_number = 1.1.1.6
| EC_number = 3.2.1.14
| CAS_number =
| CAS_number =
| IUBMB_EC_number = 1/1/1/6
| IUBMB_EC_number = 3/2/1/14
| GO_code = 0008888
| GO_code =
| image =
| image =
| width =
| width =

Revision as of 09:48, 22 January 2012

Chitinase from barley seeds
Chitinase
Identifiers
EC no.3.2.1.14
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
chitinase, acidic
Identifiers
SymbolCHIA
NCBI gene27159
HGNC17432
OMIM606080
RefSeqNM_001040623
UniProtQ9BZP6
Other data
LocusChr. 1 p13.1-21.3
Search for
StructuresSwiss-model
DomainsInterPro
chitinase 1 (chitotriosidase)
Identifiers
SymbolCHIT1
NCBI gene1118
HGNC1936
OMIM600031
RefSeqNM_003465
UniProtQ13231
Other data
LocusChr. 1 q31-q32
Search for
StructuresSwiss-model
DomainsInterPro

Chitinases are hydrolytic enzymes that break down glycosidic bonds in chitin.[1] As chitin is a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are generally found in organisms that either need to reshape their own chitin[2] or dissolve and digest the chitin of fungi or animals.

Species distribution

Chitinivorous organisms include many bacteria[3] (Aeromonads, Bacillus, Vibrio,[4] among others), which may be pathogenic or detritivorous. They attack living arthropods, zooplankton or fungi or they may degrade the remains of these organisms.

Fungi, such as Coccidioides immitis, also possess degradative chitinases related to their role as detritivores and also to their potential as arthropod pathogens.

Chitinases are also present in plants (barley seed chitinase: PDB: 1CNS​, EC 3.2.1.14); some of these are pathogenesis related (PR) proteins that are induced 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.[5]

Function

Like cellulose, chitin is an abundant biopolymer that is relatively resistant to degradation.[6] It is typically not digested by animal, though certain fish are able to digest chitin.[7] It is currently assumed that chitin digestion by animals requires bacterial symbionts and lengthy fermentations, similar to cellulase digestion by ruminants. Nevertheless, chitinases have been isolated from the stomachs of certain mammals, including humans.[8] Chitinase activity can also be detected in human blood[9][10][10] and possibly cartilage.[11] As in plant chitinases this may be related to pathogen resistance.[12][13]

Clinical significance

Human chitinases may be related to allergies, and asthma has been linked to enhanced chitinase expression levels.[14][15][16][17][18]

Human chitinases may explain the link between some of the most common allergies (dust mites, mold spores - both of which contain chitin) and and worm (helminth) infections, as part of one version of the hygiene hypothesis[19][20][21] (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.[22]

See also

References

  1. ^ Jollès P, Muzzarelli RAA (1999). Chitin and Chitinases. Basel: Birkhäuser. ISBN 3764358157.
  2. ^ Sámi L, Pusztahelyi T, Emri T, Varecza Z, Fekete A, Grallert A, Karanyi Z, Kiss L, Pócsi I (2001). "Autolysis and aging of Penicillium chrysogenum cultures under carbon starvation: Chitinase production and antifungal effect of allosamidin". The Journal of General and Applied Microbiology. 47 (4): 201–211. doi:10.2323/jgam.47.201. PMID 12483620. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  3. ^ Xiao X, Yin X, Lin J, Sun L, You Z, Wang P, Wang F (2005). "Chitinase Genes in Lake Sediments of Ardley Island, Antarctica". Applied and Environmental Microbiology. 71 (12): 7904–9. doi:10.1128/AEM.71.12.7904-7909.2005. PMC 1317360. PMID 16332766. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  4. ^ Hunt DE, Gevers D, Vahora NM, Polz MF (2008). "Conservation of the Chitin Utilization Pathway in the Vibrionaceae". Applied and Environmental Microbiology. 74 (1): 44–51. doi:10.1128/AEM.01412-07. PMC 2223224. PMID 17933912. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  5. ^ Salzer P, Bonanomi A, Beyer K, Vögeli-Lange R, Aeschbacher RA, Lange J, Wiemken A, Kim D, Cook DR, Boller T (2000). "Differential expression of eight chitinase genes in Medicago truncatula roots during mycorrhiza formation, nodulation, and pathogen infection". Molecular Plant-Microbe Interactions : MPMI. 13 (7): 763–77. doi:10.1094/MPMI.2000.13.7.763. PMID 10875337. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  6. ^ Akaki C, Duke GE (2005). "Apparent chitin digestibilities in the Eastern screech owl (Otus asio) and the American kestrel (Falco sparverius)". Journal of Experimental Zoology. 283 (4–5): 387–393. doi:10.1002/(SICI)1097-010X(19990301/01)283:4/5<387::AID-JEZ8>3.0.CO;2-W.
  7. ^ Gutowska MA, Drazen JC, Robison BH (2004). "Digestive chitinolytic activity in marine fishes of Monterey Bay, California". Comparative biochemistry and physiology. Part A, Molecular & Integrative Physiology. 139 (3): 351–8. doi:10.1016/j.cbpb.2004.09.020. PMID 15556391. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  8. ^ Paoletti MG, Norberto L, Damini R, Musumeci S (2007). "Human gastric juice contains chitinase that can degrade chitin". Annals of Nutrition & Metabolism. 51 (3): 244–51. doi:10.1159/000104144. PMID 17587796.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  9. ^ Renkema GH, Boot RG, Muijsers AO, Donker-Koopman WE, Aerts JM (1995). "Purification and Characterization of Human Chitotriosidase, a Novel Member of the Chitinase Family of Proteins". The Journal of Biological Chemistry. 270 (5): 2198–202. doi:10.1074/jbc.270.5.2198. PMID 7836450. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  10. ^ a b Escott GM, Adams DJ (1995). "Chitinase activity in human serum and leukocytes". Infection and Immunity. 63 (12): 4770–3. PMC 173683. PMID 7591134. {{cite journal}}: Unknown parameter |month= ignored (help)
  11. ^ Hakala BE, White C, Recklies AD (1993). "Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family". The Journal of Biological Chemistry. 268 (34): 25803–25810. PMID 8245017.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  12. ^ Recklies AD, White C, Ling H (2002). "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". The Biochemical Journal. 365 (Pt 1): 119–26. doi:10.1042/BJ20020075. PMC 1222662. PMID 12071845. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  13. ^ van Eijk M, van Roomen CPAA, Renkema GH, Bussink AP, Andrews L, Blommaart EFC, Sugar A, Verhoeven AJ, Boot RG, Aerts JMFG (2005). "Characterization of human phagocyte-derived chitotriosidase, a component of innate immunity". International Immunology. 17 (11): 1505–1512. doi:10.1093/intimm/dxh328. PMID 16214810.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  14. ^ Bierbaum S, Nickel R, Koch A, Lau S, Deichmann KA, Wahn U, Superti-Furga A, Heinzmann A (2005). "Polymorphisms and Haplotypes of Acid Mammalian Chitinase Are Associated with Bronchial Asthma". American Journal of Respiratory and Critical Care Medicine. 172 (12): 1505–9. doi:10.1164/rccm.200506-890OC. PMC 2718453. PMID 16179638. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  15. ^ Zhao J, Zhu H, Wong CH, Leung KY, Wong WS (2005). "Increased lungkine and chitinase levels in allergic airway inflammation: a proteomics approach". Proteomics. 5 (11): 2799–807. doi:10.1002/pmic.200401169. PMID 15996009. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  16. ^ Elias JA, Homer RJ, Hamid Q, Lee CG (2005). "Chitinases and chitinase-like proteins in T(H)2 inflammation and asthma". The Journal of Allergy and Clinical Immunology. 116 (3): 497–500. doi:10.1016/j.jaci.2005.06.028. PMID 16159614. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  17. ^ Zhu Z, Zheng T, Homer RJ, Kim YK, Chen NY, Cohn L, Hamid Q, Elias JA (2004). "Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation". Science. 304 (5677): 1678–82. doi:10.1126/science.1095336. PMID 15192232. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  18. ^ 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 (2005). "A Chitinase-like Protein in the Lung and Circulation of Patients with Severe Asthma". The New England Journal of Medicine. 357 (20): 2016–2027. doi:10.1056/NEJMoa073600. PMID 18003958.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  19. ^ Maizels RM (2005). "Infections and allergy — helminths, hygiene and host immune regulation". Current Opinion in Immunology. 17 (6): 656–61. doi:10.1016/j.coi.2005.09.001. PMID 16202576. {{cite journal}}: Unknown parameter |month= ignored (help)
  20. ^ Hunter MM, McKay DM (2004). "Review article: helminths as therapeutic agents for inflammatory bowel disease". Alimentary Pharmacology & Therapeutics. 19 (2): 167–77. doi:10.1111/j.0269-2813.2004.01803.x. PMID 14723608. {{cite journal}}: Unknown parameter |month= ignored (help)
  21. ^ Palmas C, Gabriele F, Conchedda M, Bortoletti G, Ecca AR (2003). "Causality or coincidence: may the slow disappearance of helminths be responsible for the imbalances in immune control mechanisms?". Journal of Helminthology. 77 (2): 147–53. doi:10.1079/JOH2003176. PMID 12756068. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  22. ^ Feingold BF (1975). "Food additives in clinical medicine". International Journal of Dermatology. 14 (2): 112–4. doi:10.1111/j.1365-4362.1975.tb01426.x. PMID 1123257. {{cite journal}}: Unknown parameter |month= ignored (help)

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