Taxonomic group: fungi /
Organ / tissue: cell wall
NCBI PubMed ID: 24095741Publication DOI: 10.1016/j.biotechadv.2013.09.012Journal NLM ID: 8403708Publisher: Oxford: Elsevier Science
Correspondence: faramarz

tums.ac.ir
Institutions: Department of Pharmaceutical Biotechnology, School of Pharmacy, Shahid Beheshti University of Medical Sciences, Tehran, Iran, Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center, Tehran University of Medical Sciences, Tehran, Iran
Chitinases, the enzymes responsible for the biological degradation of chitin, are found in a wide range of organisms from bacteria to higher plants and animals. They participate in numerous physiological processes such as nutrition, parasitism, morphogenesis and immunity. Many organisms, in addition to chitinases, produce inactive chitinase-like lectins that despite lacking enzymatic activity are involved in several regulatory functions. Most known chitinases belong to families 18 and 19 of glycosyl hydrolases, however a fewchitinases that belong to families 23 and 48 have also been identified in recent years. In this review, different aspects of chitinases and chi-lectins from bacteria, fungi, insects, plants and mammals are discussed.
Biomarker, chitinase, chi-lectin, gene evolution, biocontrol
Structure type: structural motif or average structure
Location inside paper: p. 1786, column 1, paragraph 1
Trivial name: chitin
Compound class: cell wall polysaccharide, glucan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85
Enzymes that release or process the structure: chitinases(GH18), β-N-acetylhexosaminidases
Biosynthesis and genetic data: biochemical data
Related record ID(s): 44855, 44856, 44877, 44889, 44899, 44913, 44916, 44917, 44923, 44925, 44940, 44941
NCBI Taxonomy refs (TaxIDs): 4751Reference(s) to other database(s): GTC:G97099AY
Show glycosyltransferases
There is only one chemically distinct structure: