Editing Chitinase (section)

== Species distribution ==

Chitinivorous organisms include many bacteria<ref name="pmid16332766">{{cite journal | vauthors = Xiao X, Yin X, Lin J, Sun L, You Z, Wang P, Wang F | title = Chitinase genes in lake sediments of Ardley Island, Antarctica | journal = Applied and Environmental Microbiology | volume = 71 | issue = 12 | pages = 7904–9 | date = December 2005 | pmid = 16332766 | pmc = 1317360 | doi = 10.1128/AEM.71.12.7904-7909.2005 | bibcode = 2005ApEnM..71.7904X }}</ref> ([[Aeromonadales|Aeromonad]]s, ''[[Bacillus]]'', ''[[Vibrio]]'',<ref name="pmid17933912">{{cite journal | vauthors = Hunt DE, Gevers D, Vahora NM, Polz MF | title = Conservation of the chitin utilization pathway in the Vibrionaceae | journal = Applied and Environmental Microbiology | volume = 74 | issue = 1 | pages = 44–51 | date = January 2008 | pmid = 17933912 | pmc = 2223224 | doi = 10.1128/AEM.01412-07 | bibcode = 2008ApEnM..74...44H }}</ref> among others), which may be [[pathogenic]] or detritivorous.  They attack living [[arthropod]]s, [[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 – for example [[barley]] seed chitinase: {{PDB|1CNS}}, {{EC number|3.2.1.14}}. Barley seeds are found to produce [[clone 10]] in Ignatius et al 1994(a). They find clone 10, a [[Class I chitinase]], in the seed [[aleurone]] during development.<ref name="Muthukrishnan-et-al-2001">{{cite journal | vauthors = Muthukrishnan S, Liang GH, Trick HN, Gill BS | journal=[[Plant Cell, Tissue and Organ Culture]] | publisher=[[Kluwer Academic]] | volume=64 | issue=2/3 | year=2001 | issn=0167-6857 | doi=10.1023/a:1010763506802 | pages=93–114 | title=Pathogenesis-related proteins and their genes in cereals| s2cid=43466565 }}</ref><ref name="Gomez-et-al-2002">{{cite journal | vauthors = Gomez L, Allona I, Casado R, Aragoncillo C | title=Seed chitinases | journal=[[Seed Science Research]] | publisher=[[Cambridge University Press]] (CUP) | volume=12 | issue=4 | year=2002 | issn=0960-2585 | doi=10.1079/ssr2002113 | pages=217–230| s2cid=233361411 }}</ref><ref name="Waniska-et-al-2001">{{cite journal | vauthors = Waniska RD, Venkatesha RT, Chandrashekar A, Krishnaveni S, Bejosano FP, Jeoung J, Jayaraj J, Muthukrishnan S, Liang GH | display-authors = 6 | title = Antifungal proteins and other mechanisms in the control of sorghum stalk rot and grain mold | journal = Journal of Agricultural and Food Chemistry | volume = 49 | issue = 10 | pages = 4732–4742 | date = October 2001 | pmid = 11600015 | doi = 10.1021/jf010007f | publisher = [[American Chemical Society]] (ACS) }}</ref> Leaves produce several [[isozyme]]s (as well as several of [[β-1,3-glucanase]]). Ignatius et al 1994(b) find these in the leaves, induced by [[powdery mildew of barley|powdery mildew]].<ref name="Muthukrishnan-et-al-2001" /> Ignatius et al also find these (seed and leaf isozymes) to differ from each other.<ref name="Gomez-et-al-2002" /><ref name="Basra-2007">{{cite book | first= A.S. |last=Basra | title=Handbook of Seed Science and Technology | publisher=Scientific Publishers | year=2007 | isbn=978-93-88148-36-8 | url=https://books.google.com/books?id=mNaBDwAAQBAJ | access-date=2021-11-17 | pages=795 |doi=10.2307/25065722 |jstor=25065722 | section=3. Seed Ecology Chapter 16. Natural defense mechanisms in seeds | s2cid=83869430}} {{ISBN|9788172335731}} {{ISBN|9388148363}}.</ref> Some of these are [[pathogenesis related (PR) proteins]] that are [[Enzyme induction and inhibition|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.<ref name="pmid10875337">{{cite journal | vauthors = Salzer P, Bonanomi A, Beyer K, Vögeli-Lange R, Aeschbacher RA, Lange J, Wiemken A, Kim D, Cook DR, Boller T | display-authors = 6 | title = Differential expression of eight chitinase genes in ''Medicago truncatula'' roots during mycorrhiza formation, nodulation, and pathogen infection | journal = Molecular Plant-Microbe Interactions | volume = 13 | issue = 7 | pages = 763–777 | date = July 2000 | pmid = 10875337 | doi = 10.1094/MPMI.2000.13.7.763 | doi-access = free }}</ref>

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 [[CHI3L1|YKL-40]]) that have high sequence similarity but lack chitinase activity.<ref>{{cite journal | vauthors = Eurich K, Segawa M, Toei-Shimizu S, Mizoguchi E | title = Potential role of chitinase 3-like-1 in inflammation-associated carcinogenic changes of epithelial cells | journal = World Journal of Gastroenterology | volume = 15 | issue = 42 | pages = 5249–59 | date = November 2009 | pmid = 19908331 | pmc = 2776850 | doi = 10.3748/wjg.15.5249 | doi-access = free }}</ref>