キチナーゼ

オオムギ種子のキチナーゼ
キチナーゼ
識別子
EC番号 3.2.1.14
データベース
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB構造 RCSB PDB PDBj PDBe PDBsum
検索
PMC articles
PubMed articles
NCBI proteins
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chitinase, acidic
識別子
略号 CHIA
Entrez（英語版） 27159
HUGO 17432
OMIM 606080
RefSeq NM_001040623
UniProt Q9BZP6
他のデータ
遺伝子座 Chr. 1 p13.1-21.3
テンプレートを表示
chitinase 1 (chitotriosidase)
識別子
略号 CHIT1
Entrez（英語版） 1118
HUGO 1936
OMIM 600031
RefSeq NM_003465
UniProt Q13231
他のデータ
遺伝子座 Chr. 1 q31-q32
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キチナーゼ(Chitinase、EC 3.2.1.14)は、キチンのグリコシド結合を分解する加水分解酵素である[1]。キチンは菌の細胞壁及びいくつかの種の動物（蠕虫、節足動物）の外骨格を形成する成分であるため、キチナーゼは自身のキチンを再構成する必要のある生物か[2]、菌または動物のキチンを消化する必要のある生物が持つ。

種の分布

キチンを食べる生物には、病原性または腐食性の多くの細菌（エアロモナス目、バシラス属、ビブリオ属[3]、その他）が含まれる[4]。生きた節足動物、動物プランクトン、菌に直接作用することもあれば、それらの生物の残骸に作用することもある。

Coccidioides immitis等の菌は、デトリタス食及び節足動物に対する病原性の発現のためにこの酵素を持つ。

キチナーゼは、オオムギの種子(PDB: 1CNS​)等、植物でも見られることがある。それらの一部は、感染特異的タンパク質で、生体防御の一部として誘導される。発現は、どちらも菌や昆虫の攻撃からの防御に関連するNPR1遺伝子とサリチル酸経路によって仲介される。植物のキチナーゼには、他に菌との共生に必要なものもある[5]。

ほ乳類はキチンを生成しないが、2つの活性を持つキチナーゼ（キトトリオシダーゼと酸性ほ乳類キチナーゼ）を有する。他に、配列の類似性は高いがキチナーゼ活性を持たないYKL-40等がある[6]。

機能

セルロースと同様に、キチンは比較的分解されにくく、豊富に存在する生体高分子である[7]。通常、動物はこれを消化することはできないが、ある種の魚類は消化することができる[8]。動物によるキチンの消化には、反芻動物のセルロースの消化と同様に、細菌との共生及び非常に長い発酵時間が必要だと考えられている。それにも関わらず、キチナーゼは、ヒトを含む動物の胃から単離されている[9]。キチナーゼ活性はヒトの血液[10][11][11]や恐らくは軟骨でも検出できる[12]。植物のキチナーゼは、病原性への抵抗と関わっている[13][14]。

医療上の重要性

ヒトのキチナーゼは、アレルギーと関わっており、気管支喘息はキチナーゼの発現レベルの亢進と関係がある[15][16][17][18][19]。

ヒトのキチナーゼは、どちらもキチンを持つイエダニやカビの胞子によるアレルギーと寄生蠕虫の感染を結びつけている（蠕虫は、腸壁に固定するためのキチン質の口部を持っている）[20][21][22]。キチナーゼと植物のサリチル酸経路の間の関連は解明されたが、サリチル酸経路とヒトのアレルギーの間には、未解明の部分が残っている[23]。

食物中の存在

キチナーゼは、食物の中にも含まれている。これは、ラテックスフルーツ症候群の少なくとも原因の1つになっている。例えばバナナ、クルミ、キウイフルーツ、アボカド、パパイア、トマト等は、かなりの量のキチナーゼを含んでいる。その他には、ナガイモなどがある。[24]

関連項目

出典

  1. ^ Jolles P, Muzzarelli RAA (1999). Chitin and Chitinases. Basel: Birkhauser. ISBN 3-7643-5815-7 
  2. ^ Sami L, Pusztahelyi T, Emri T, Varecza Z, Fekete A, Grallert A, Karanyi Z, Kiss L, Pocsi I (August 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. 
  3. ^ Hunt DE, Gevers D, Vahora NM, Polz MF (January 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2223224/. 
  4. ^ Xiao X, Yin X, Lin J, Sun L, You Z, Wang P, Wang F (December 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1317360/. 
  5. ^ Salzer P, Bonanomi A, Beyer K, Vogeli-Lange R, Aeschbacher RA, Lange J, Wiemken A, Kim D, Cook DR, Boller T (July 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. 
  6. ^ Eurich, K; et al. (2009 Nov). “Potential role of chitinase 3-like-1 in inflammation-associated carcinogenic changes of epithelial cells.”. World J Gastroenterol 15 (42): 5249?5259. PMC 2776850. PMID 19908331. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2776850/. 
  7. ^ 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. 
  8. ^ Gutowska MA, Drazen JC, Robison BH (November 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. 
  9. ^ 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. 
  10. ^ Renkema GH, Boot RG, Muijsers AO, Donker-Koopman WE, Aerts JM (February 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. 
  11. ^ a b Escott GM, Adams DJ (December 1995). “Chitinase activity in human serum and leukocytes”. Infection and Immunity 63 (12): 4770?3. PMC 173683. PMID 7591134. http://iai.asm.org/cgi/pmidlookup?view=long&pmid=7591134. 
  12. ^ 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. 
  13. ^ Recklies AD, White C, Ling H (July 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222662/. 
  14. ^ 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. 
  15. ^ Bierbaum S, Nickel R, Koch A, Lau S, Deichmann KA, Wahn U, Superti-Furga A, Heinzmann A (December 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2718453/. 
  16. ^ Zhao J, Zhu H, Wong CH, Leung KY, Wong WS (July 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. 
  17. ^ Elias JA, Homer RJ, Hamid Q, Lee CG (September 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. 
  18. ^ 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”. Science 304 (5677): 1678?82. doi:10.1126/science.1095336. PMID 15192232. 
  19. ^ 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. 
  20. ^ Maizels RM (December 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. 
  21. ^ Hunter MM, McKay DM (January 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. 
  22. ^ 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?”. Journal of Helminthology 77 (2): 147?53. doi:10.1079/JOH2003176. PMID 12756068. 
  23. ^ Feingold BF (March 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. 
  24. ^ 古賀大三「植物キチナーゼと生体防御」『化学と生物』第32巻第11号、日本農芸化学会、1994年、712-722頁、doi:10.1271/kagakutoseibutsu1962.32.712、2016年2月6日閲覧。 

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