Chitinase

Chitinase
Serratia marcescens chitinase A dimer with bound inhibitor allosamidin. PDB: 1FFQ
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
Homo sapiens acidic mammalian chitinase with bound inhibitor methylallosamidin. PDB: 3FY1
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)
Homo sapiens chitotriosidase bound with two molecules of inhibitor allosamidin PDB: 1HKK
Identifiers
SymbolCHIT1
NCBI gene1118
HGNC1936
OMIM600031
RefSeqNM_003465
UniProtQ13231
Other data
LocusChr. 1 q31-q32
Search for
StructuresSwiss-model
DomainsInterPro

Chitinases (EC 3.2.1.14, chitodextrinase, 1,4-β-poly-N-acetylglucosaminidase, poly-β-glucosaminidase, β-1,4-poly-N-acetyl glucosamidinase, poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase, (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase; systematic name (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase) are hydrolytic enzymes that break down glycosidic bonds in chitin.[1] They catalyse the following reaction:

Random endo-hydrolysis of N-acetyl-β-D-glucosaminide (1→4)-β-linkages in chitin and chitodextrins

As chitin is a component of the cell walls of fungi and exoskeletal elements of some animals (including mollusks 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.

  1. ^ Jollès P, Muzzarelli RA (1999). Chitin and Chitinases. Basel: Birkhäuser. ISBN 978-3-7643-5815-0.
  2. ^ Sámi L, Pusztahelyi T, Emri T, Varecza Z, Fekete A, Grallert A, Karanyi Z, Kiss L, Pócsi 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.