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Enzyme Nomenclature
Information on EC 3.2.1.14 - chitinase
for references in articles please use BRENDA:EC3.2.1.14
Word Map on EC 3.2.1.14
- 3.2.1.14
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antifungal
- fungus
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colloidal
- trichoderma
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biocontrol
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chitin-binding
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pathogenesis-related
- serratia
- fusarium
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freezing
- marcescens
- gaucher
- beta-1,3-glucanase
- solani
- n-acetylglucosamine
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3-like
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phytopathogenic
- rhizoctonia
- glcnac
- harzianum
- cinerea
- cellulase
- oxysporum
- botrytis
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glucanase
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elicitors
- mycelial
- hyphal
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hysteresis
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defense-related
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rhizosphere
- colletotrichum
- circulans
- flounder
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molt
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entomopathogenic
- n-acetyl-d-glucosamine
- chitosanase
- viride
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4-methylumbelliferyl
- sclerotinia
- metarhizium
- glucocerebrosidase
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transglycosylation
- sclerotiorum
- beauveria
- nucleopolyhedrovirus
- bassiana
- hevea
- rhizobacteria
- environmental protection
- molecular biology
- analysis
- synthesis
- industry
- degradation
- biotechnology
- medicine
- pharmacology
- agriculture
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.2.1.14
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RECOMMENDED NAME
GeneOntology No.
chitinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
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Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
the enzyme shows endo- and exo-hydrolytic activity, as well as transglycosylation activity
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Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
exo-type substrate cleavage mechanism
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Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
catalytic reaction mechanism involving Glu119, overview
Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
reaction mechanism, Glu315 is the acid/base during hydrolysis, the side-chain of the preceding Asp313 helps to position the N-acetyl moiety of the glycosyl sugar undergoing hydrolysis correctly, mutation of the conserved Tryp167 in the chitin-binding cleft of chitinase A enhances transglycosylation, transglycosylation reaction scheme, overview
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Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
catalytic mechanism, overview
Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
mode of action of ChiG, family 19 chitinases use a single-displacement reaction with inversion of the configuration of the anomeric carbon, overview
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Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
catalytic mechanism with an important role of Trp-33 on enzyme processivity, CHI60 preferentially uses the endo-type mode on soluble and amorphous substrates and the exo-type mode on crystalline substrate, the enzyme hydrolyzes crystalline substrates with an exo-type mode processively while remaining tightly bound to the substrate. The prevalent mode of hydrolysis mediated by CHI60 is regulated by ionic strength
Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
chitooligosaccharide-binding modes and catalytic mechanism, overview
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Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
double displacement reaction mechanism, overview
Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
the enzyme shows endo- and exo-hydrolytic activity, as well as transglycosylation activity
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Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
double displacement reaction mechanism, overview
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Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
catalytic mechanism with an important role of Trp-33 on enzyme processivity, CHI60 preferentially uses the endo-type mode on soluble and amorphous substrates and the exo-type mode on crystalline substrate, the enzyme hydrolyzes crystalline substrates with an exo-type mode processively while remaining tightly bound to the substrate. The prevalent mode of hydrolysis mediated by CHI60 is regulated by ionic strength
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Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
mode of action of ChiG, family 19 chitinases use a single-displacement reaction with inversion of the configuration of the anomeric carbon, overview
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Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
exo-type substrate cleavage mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase
The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo-chitodextrinases can act. Activity is greatly stimulated in the presence of EC 1.14.99.53, lytic chitin monoxygenase, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase. cf. EC 3.2.1.202, endo-chitodextrinase.
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CAS REGISTRY NUMBER
COMMENTARY
9001-06-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from a soil sample collected from hot spring of XinJiang Province, China
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isolated from natto, a traditional Japanese food, 3 isozymes Chi1-3
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diverse strains, isolated from environmental sources, water or a Sphagnum pond, overview
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diverse strains, isolated from environmental sources, water or a Sphagnum pond, overview
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different strins, genes chiA, chiB, chiC, and chiD
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arbiscular mycorrhizal fungus inoculated in roots of grapevine, Vitis amurensis, gene VCH3
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DSM 21863, CCTCC AB208287, gene chiB encoding isozyme Is-chiB
UniProt
DSM 21863, CCTCC AB208287, gene chiB encoding isozyme Is-chiB
UniProt
ssp. lactis, strain IL1403, a derivative of the strain IL594 that is isolated from a cheese starter culture, gene LlChi18A
UniProt
diverse strains and serotypes, overview. Strain EGD, two isozymes lmo0105 and lmo1883, encoded by genes chiB and chiA, respectively
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desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
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plant pathogen, strains 9713 and Temecula in Vinis sp., and strains 9a5c, SR3, and SR28 in Citrus sp., secreted serine- and metallo-protease with chitinase activity
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isolated from a soil sample collected from hot spring of XinJiang Province, China
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gene Chi-h encodes an exochitinase, the organism also contains an endochitinase
SwissProt
several different cultuvars, e.g. metal-tolerant cv. Chernyatka and the metal-sensitive cv. Kyivska 98
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genes chiA, chiB, and chiC encoding isozymes BJL200-ChiA, BJL200-ChiB, and BJL200-ChiC, respectively
UniProt
genes chiA, chiB, and chiC encoding isozymes BJL200-ChiA, BJL200-ChiB, and BJL200-ChiC, respectively
UniProt
11 putative family 18 chitinases and two putative family 19 chitinases, ChiF and ChiG
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13 genes encoding 11 enzyme from chitinase family 18 and 19, overview
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11 putative family 18 chitinases and two putative family 19 chitinases, ChiF and ChiG
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13 genes encoding 11 enzyme from chitinase family 18 and 19, overview
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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BcChi-A is glycoside hydrolase family-19 chitinase lacking loops I, II, IV and V, and a C-terminal loop, which are present in the catalytic domain of plant class I and II chitinases. The phylogenetic relationships of BcChi-A and other GH19 chitinases shows that BcChi-A is closely related to GH19 chitinases from bacteria
evolution
the enzyme belongs to the glycosyl hydrolase family 18 (GH18) of chitinases
evolution
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the enzyme belongs to the glycosyl hydrolase family GH19
evolution
phylogenetic analysis reveals the possibility of horizontal gene transfer between bacteria, viruses, and insects. The Chit62 enzyme is clearly grouped with other bacterial chitinases, but with a clear distinction from previously reported Serratia marcescens
evolution
the enzyme belongs to the glycosyl hydrolase family GH18; the enzyme belongs to the glycosyl hydrolase family GH18; the enzyme belongs to the glycosyl hydrolase family GH18; the enzyme belongs to the glycosyl hydrolase family GH18; the enzymes of the operon chiCDEFG belong to the glycosyl hydrolase family GH18, while chiF encodes a polypeptide with two chitin-binding domains, but no catalytic domain
evolution
the enzyme belongs to the glycosyl hydrolase family GH 19
evolution
the enzyme is a typical glycoside hydrolase family 18 chitinase
evolution
the enzyme belongs to carbohydrate-binding module family 18 and glycoside hydrolase family GH19. Possibly the two proteins class IV chitinase and class IV endochitinase, UniProt IDs Q7XAU6 and O24530, are allelic variants encoded by the same gene
evolution
the enzyme belongs to the glycosyl hydrolase family GH23, that also includes goose-type (G-type) lysozymes, peptidoglycan lyases, and peptidoglycan lytic transglycosylases. It has a catalytic domain sequence similar to goose-type (G-type) lysozymes, the unique arrangement of the catalytic residues makes a clear contrast to the other GH23 members and also to inverting GH19 chitinases. Enzyme Ra-ChiC produces alpha-anomers by hydrolyzing beta-1,4-glycosidic linkages, indicating that the enzyme is an inverter like GH family 19 chitinases
evolution
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evolutionary adaptation of soybean to environmental cues, i.e. metal toxicity stress
evolution
the enzyme belongs to the glycosyl hydrolase family GH18
evolution
the enzyme is a glycoside hydrolase family 19 plant class IV chitinase. Family GH19 chitinases operate by an inverting glycoside mechanism. Comparison of the crystal structure of this plant class IV chitinase with structures from larger class I and II enzymes suggest that class IV chitinases have evolved to accommodate shorter substrates
evolution
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the enzyme belongs to the glycosyl hydrolase family GH18
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evolution
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the enzyme belongs to the glycosyl hydrolase family GH18; the enzyme belongs to the glycosyl hydrolase family GH18; the enzyme belongs to the glycosyl hydrolase family GH18; the enzyme belongs to the glycosyl hydrolase family GH18; the enzymes of the operon chiCDEFG belong to the glycosyl hydrolase family GH18, while chiF encodes a polypeptide with two chitin-binding domains, but no catalytic domain
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evolution
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the enzyme is a typical glycoside hydrolase family 18 chitinase
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evolution
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the enzyme belongs to the glycosyl hydrolase family GH19
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evolution
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the enzyme belongs to the glycosyl hydrolase family GH23, that also includes goose-type (G-type) lysozymes, peptidoglycan lyases, and peptidoglycan lytic transglycosylases. It has a catalytic domain sequence similar to goose-type (G-type) lysozymes, the unique arrangement of the catalytic residues makes a clear contrast to the other GH23 members and also to inverting GH19 chitinases. Enzyme Ra-ChiC produces alpha-anomers by hydrolyzing beta-1,4-glycosidic linkages, indicating that the enzyme is an inverter like GH family 19 chitinases
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evolution
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phylogenetic analysis reveals the possibility of horizontal gene transfer between bacteria, viruses, and insects. The Chit62 enzyme is clearly grouped with other bacterial chitinases, but with a clear distinction from previously reported Serratia marcescens
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evolution
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the enzyme belongs to carbohydrate-binding module family 18 and glycoside hydrolase family GH19. Possibly the two proteins class IV chitinase and class IV endochitinase, UniProt IDs Q7XAU6 and O24530, are allelic variants encoded by the same gene
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evolution
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the enzyme is a glycoside hydrolase family 19 plant class IV chitinase. Family GH19 chitinases operate by an inverting glycoside mechanism. Comparison of the crystal structure of this plant class IV chitinase with structures from larger class I and II enzymes suggest that class IV chitinases have evolved to accommodate shorter substrates
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malfunction
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isozyme YlCts1p deletion results in remarkably reduced extracellular endochitinase activity in the culture supernatant of Yersinia lipolytica and enhanced cell aggregation
malfunction
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insertional inactivation of a chi54 locus in mutant C61Chi54M abolishes growth on chitin as a sole carbon source, enzyme activity is not detected
malfunction
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insertional inactivation of a chi54 locus in mutant C61Chi54M abolishes growth on chitin as a sole carbon source, enzyme activity is not detected
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metabolism
the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation; the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation; the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation; the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation; the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation
metabolism
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activities of the individual chitinases are dependent on the metal type as well as the cultivar pointing to their more complex role in plant defense during this type of stress
metabolism
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the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation; the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation; the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation; the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation; the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation
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physiological function
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expression of chitinase in Bacillus thuringiensis under the control of a strong promoter and a 5'-mRNA stabilizing sequence leads to markedly elevated chinolytic activity and a diminution of 10-20% in size of the crystals produced. Strains overexpressing chitinase produce fewer viable spores. No change in protease activity is observed depsite teh overproduction of chitinase
physiological function
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enzyme has potent inhibitory action toward fungal species including Botrytis cinerea, Physalospora piricola, Fusarium oxysporum, and Pythium aphanidermatum
physiological function
enzyme consists of a catalytic domain, a fibronectin type III domain, and a chitin binding domain. The catalytic domain with one amino acid in C-terminal region is sufficient for chitinase activity. The C-terminus is important in binduing to shell powder
physiological function
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endochitinases Chi2, Chi22 actively degrade chitinoligomeric substrates. A mutant strain lacking isoforms chi2, chi21, chi22, chi4 is unable to cleave 4-methylumbelliferyl-(GlcNAc)3. Strains containing only Chi4 or Chi21 also show no activity on 4-methylumbelliferyl-(GlcNAc)3. A strain containing only the endochitinase Chi22 has measurable activity against 4-methylumbelliferyl-(GlcNAc)3 when the cells are grown on either GlcNAc or glucose as a carbon source, although less on the glucose carbon source. A strain containing only Chi2 has measurable activity when grown on both glucose and GlcNAc Chi2, Chi21, and Chi4 are each involved in sexual reproduction
physiological function
enzyme exhibits in vitro antifungal activity against Botrytis cinerea and is able to cryoprotect lactate dehydrogenase against freeze/thaw inactivation
physiological function
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purified ChiA enhances the permeability of the peritrophic membrane of larvae of Lepidoptera Bombyx mori and Heliothis virescens and inhibits spore germination and growth of the phytopatogenic fungus Alternaria alternata
physiological function
enzyme efficiently degrades cell wall chitin of the phytopathogenic Rhizoctonia solani, Fusarium oxysporum, Sclerotinia sclerotiorum, Valsa sordida, Septoria tritici and Phytophthora sojae
physiological function
class IV enzymes are optimized for shorter substrates than the class I and II enzymes, or alternatively, they are better suited for action on substrates where only small regions of chitin chain are accessibl. The intact enzyme shows antifungal acivtiy, while the catalytic subunit alone has very low antifungal activity
physiological function
chitinase can damage eggs of both the root-knot nematode Meloidogyne incognita and the insect Bombyx mori
physiological function
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chitinases are glycoside hydrolases that catalyze the degradation of chitin, a linear beta-1,4-linked polymer of N-acetylglucosamine
physiological function
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the viral chitinase is involved in the final liquefaction of the infected host larvae
physiological function
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ChiA significantly inhibits the spore germination of four species of fungi. The IC50 of ChiA on the spore germination of Penicillium glaucum and Sclerotinia fuckelian are 0.0113 mg/ml and 0.0106 mg/ml, respectively. The crude ChiA protein at 12.6 mU reduced the LC50 of the crystal protein of strain 15A3 against the larvae of Spodoptera exigua and Helicoverpa armigera
physiological function
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chitinase hydrolyzes the beta-1,4 glycosidic bond of chitin, the linear polysaccharide of GlcNAc, to produce chitooligosaccharides
physiological function
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the purified enzyme inhibits the growth of fungal phytopathogens belonging to the genera Fusarium, Rhizoctonia and Alternaria
physiological function
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BChi14 is functionally implicated in the mechanisms underlying chilling tolerance activated by high CO2 concentrations. The purified endochitinase shows very strong cryoprotective activity against freeze-thaw inactivation of lactate dehydrogenase, but the enzyme has no effect on the inhibition of Botrytis cinerea hyphal growth and no antifreeze activity
physiological function
chitinases are a group of enzymes capable of hydrolysing the bta-(1,4)-glycosidic bonds of chitin, an essential component of the fungal cell wall, the shells of nematode eggs, and arthropod exoskeletons
physiological function
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sAMC has a role in conversion of chitin wastes into useful products. It also exhibits antifungal activity against Trichoderma viride, Botrytis cinerea, Fusarium oxysporum and Fusarium solani
physiological function
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the purified antifungal alkaline chitinase exhibits remarkable antifungal activity against pathogenic fungi Aspergillus flavus MTCC 2798 and Aspergillus niger MTCC 9652
physiological function
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the enzyme exhibits antifungal activity against phytopathogenic and human pathogenic fungi
physiological function
the active enzyme shows biocontrol features against fungal phytopathogens
physiological function
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chitinolytic enzymes attack chitin contained in the cell walls of plant pathogenic fungi and then impair the growth of fungi living in soil. Biodegradation of shrimp head powder by the chitinase of Bacillus cereus TKU028 is conducive to the growth of strain TKU028 and the coexisting bacteria
physiological function
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the chitinase from the stomach of the red scorpionfish Scorpaena scrofa has bioinsecticidal activity toward cowpea weevil Callosobruchus maculatus
physiological function
recombinant Pichia pastoris-produced chitinase shows strong lytic activity against Fusarium oxysporum and Phytophthora nicotianae
physiological function
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plant chitinases are considered to be pathogen related proteins used to defend against invasions such as external fungi and insects attacks, that contain chitins
physiological function
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chitinase cleaves the beta-1,4-linkage between N-acetyl-D-glucosamine residues in the linear homopolymer chitin, which is an essential component of yeast and fungal cell walls
physiological function
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strain C61 displays antifungal activities in vitro. Purified chitinase inhibits spore germination of multiple pathogens. Culture filtrates of the wild-type Chromobacterium sp. C61 and the mutant C61Chi54TS, that has a higer activity than the wild-type, both produce significant in planta biocontrol activity against rice blast, tomato leaf blight and wheat leaf rust. The enzyme expression might be under under quorum sensing control
physiological function
the enzyme has in vitro antifungal activity in healthy maize seeds
physiological function
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in presence of lytic polysaccharide monooxygenase Cbp21, the apparent kcat values of chitinases ChiA and ChiB increase 6-9fold, while there is no effect on chitinase ChiC; in presence of lytic polysaccharide monooxygenase Cbp21, the apparent kcat values of chitinases ChiA and ChiB increase 6-9fold, while there is no effect on chitinase ChiC
physiological function
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presence of CBP21 increases solubilization of chitin substrates with high degrees of crystallinity when combined with each of the three chitinases ChiA, ChiB, or ChiC, but this synergy is reduced upon decline in crystallinity; presence of CBP21 increases solubilization of chitin substrates with high degrees of crystallinity when combined with each of the three chitinases ChiA, ChiB, or ChiC, but this synergy is reduced upon decline in crystallinity; presence of CBP21 increases solubilization of chitin substrates with high degrees of crystallinity when combined with each of the three chitinases ChiA, ChiB, or ChiC, but this synergy is reduced upon decline in crystallinity. Isoform ChiA shows lowest effects
physiological function
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enzyme inhibits the growth of phytopathogenic fungi like Fusarium oxysporum and Curvularia lunata
physiological function
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chitinolytic enzymes attack chitin contained in the cell walls of plant pathogenic fungi and then impair the growth of fungi living in soil. Biodegradation of shrimp head powder by the chitinase of Bacillus cereus TKU028 is conducive to the growth of strain TKU028 and the coexisting bacteria
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physiological function
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ChiA significantly inhibits the spore germination of four species of fungi. The IC50 of ChiA on the spore germination of Penicillium glaucum and Sclerotinia fuckelian are 0.0113 mg/ml and 0.0106 mg/ml, respectively. The crude ChiA protein at 12.6 mU reduced the LC50 of the crystal protein of strain 15A3 against the larvae of Spodoptera exigua and Helicoverpa armigera
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physiological function
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strain C61 displays antifungal activities in vitro. Purified chitinase inhibits spore germination of multiple pathogens. Culture filtrates of the wild-type Chromobacterium sp. C61 and the mutant C61Chi54TS, that has a higer activity than the wild-type, both produce significant in planta biocontrol activity against rice blast, tomato leaf blight and wheat leaf rust. The enzyme expression might be under under quorum sensing control
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physiological function
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the purified antifungal alkaline chitinase exhibits remarkable antifungal activity against pathogenic fungi Aspergillus flavus MTCC 2798 and Aspergillus niger MTCC 9652
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physiological function
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chitinases are glycoside hydrolases that catalyze the degradation of chitin, a linear beta-1,4-linked polymer of N-acetylglucosamine
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physiological function
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the enzyme exhibits antifungal activity against phytopathogenic and human pathogenic fungi
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physiological function
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the active enzyme shows biocontrol features against fungal phytopathogens
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physiological function
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the purified enzyme inhibits the growth of fungal phytopathogens belonging to the genera Fusarium, Rhizoctonia and Alternaria
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physiological function
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enzyme inhibits the growth of phytopathogenic fungi like Fusarium oxysporum and Curvularia lunata
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physiological function
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the enzyme has in vitro antifungal activity in healthy maize seeds
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additional information
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deletion of four loops likely leads the enzyme to optimize the (beta-1,4-GlcNAc)n hydrolytic reaction rather than hydrolysis of polymeric substrates
additional information
NtChiV is a non-processive enzyme. The aglycon binding site of NtChiV appears to consist of three subsites, +1, +2, and +3. Structural comparison with other family GH-18 chitinases, overview
additional information
catalytic domain structure with and without bound substrate, structure comparisons and structure-function relationship, overview
additional information
Glu691 and Glu1177 in the two GH-18 domains are catalytic residues, two catalytic domains act synergistically to degrade chitin. The reaction mechanism of ChiW is suggested to be similar to the mechanism of GH-18 chitinases, in which one glutamate residue functions as a general acid/base catalyst and a GlcNAc C-2 acetamide group of the chitin substrate at subsite -1 carries out a nucleophilic attack on the GlcNAc C-1 carbon atom generating an oxazoline ion intermediate. Other important residues of the chitinase subfamily A enzymes for saccharide binding and catalytic reaction are also highly conserved in the ChiW GH-18 domains: Trp568 (Trp1055), Trp905 (Trp1396), Trp652 (Trp1138), and Trp772 (Trp1258) for saccharide binding, Tyr766 (Tyr1252), Asp687 (Asp1173), and Asp689 (Asp1175) for the catalytic reaction
additional information
at a concentration and pH expected in ripe grapes, no inhibition of wine yeast growth by the chitinase is observed
additional information
structure-function analysis, highly conserved Glu141 acts as a catalytic acid, and Asp226 located at the roof of the tunnel activates a water molecule as a catalytic base, Asp226 is critical for catalysis
additional information
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isozyme YlCts1p contains an N-terminal secretion signal peptide, a long C-terminal Ser/Thr-rich domain, and a chitin-binding domain
additional information
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chitinases in Glycine max roots specifically respond to different metal types and reveal a polymorphism that coincides with sensitivity to metal toxicity
additional information
key roles for Glu62, Arg177, and Glu165 in hydrolysis, and for Ser103 and Tyr106 in substrate binding. Glu62 is directly involved in catalysis, while the hevein-like domain is not needed for enzyme activity. Proton donor and general base are Glu62 and Glu71, respectively. The catalytic triad highly conserved in GH19 chitinases, is composed of Glu62, Arg177, and Glu165
additional information
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Glu691 and Glu1177 in the two GH-18 domains are catalytic residues, two catalytic domains act synergistically to degrade chitin. The reaction mechanism of ChiW is suggested to be similar to the mechanism of GH-18 chitinases, in which one glutamate residue functions as a general acid/base catalyst and a GlcNAc C-2 acetamide group of the chitin substrate at subsite -1 carries out a nucleophilic attack on the GlcNAc C-1 carbon atom generating an oxazoline ion intermediate. Other important residues of the chitinase subfamily A enzymes for saccharide binding and catalytic reaction are also highly conserved in the ChiW GH-18 domains: Trp568 (Trp1055), Trp905 (Trp1396), Trp652 (Trp1138), and Trp772 (Trp1258) for saccharide binding, Tyr766 (Tyr1252), Asp687 (Asp1173), and Asp689 (Asp1175) for the catalytic reaction
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additional information
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structure-function analysis, highly conserved Glu141 acts as a catalytic acid, and Asp226 located at the roof of the tunnel activates a water molecule as a catalytic base, Asp226 is critical for catalysis
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additional information
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at a concentration and pH expected in ripe grapes, no inhibition of wine yeast growth by the chitinase is observed
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additional information
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key roles for Glu62, Arg177, and Glu165 in hydrolysis, and for Ser103 and Tyr106 in substrate binding. Glu62 is directly involved in catalysis, while the hevein-like domain is not needed for enzyme activity. Proton donor and general base are Glu62 and Glu71, respectively. The catalytic triad highly conserved in GH19 chitinases, is composed of Glu62, Arg177, and Glu165
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(GlcNAc)6 + H2O
(GlcNAc)2 + (GlcNAc)3 + (GlcNAc)4
the enzyme prefers the beta-anomer of chito-oligosaccharides as substrate, cleavage of beta-glycosidic linkages from the non-reducing end primarily by disaccharide units
product analysis
-
r
2-acetamido-2-deoxy-4-O-(2-acetamido-2-deoxy-4-O-methyl-beta-D-glucopyranosyl)-1-O-4-methylumbelliferyl-beta-D-glucopyranoside + H2O
?
-
-
-
-
?
2-acetamido-2-deoxy-4-O-(2-acetamido-4-O-cyclohexylmethyl-2-deoxy-beta-D-glucopyranosyl)-1-O-4-methylumbelliferyl-beta-D-glucopyranoside + H2O
?
-
-
-
-
?
2-acetamido-2-deoxy-4-O-(2-deoxy-2-acetamido-4-O-isopropyl-beta-D-glucopyranosyl)-1-O-4-methylumbelliferyl-beta-D-glucopyranoside + H2O
?
-
-
-
-
?
4-methylumbelliferyl 2-acetamido-4-O-(2-acetamido-2,4-dideoxy-beta-D-xylo-hexopyranosyl)-2-deoxy-beta-D-glucopyranoside + H2O
4-methylumbelliferol + 2-acetamido-4-O-(2-acetamido-2,4-dideoxy-beta-D-xylo-hexopyranosyl)-2-deoxy-beta-D-glucopyranoside
-
-
-
-
?
4-methylumbelliferyl beta-D-N,N',N''-triacetylchitotrioside + H2O
4-methylumbelliferol + beta-D-N,N',N''-triacetylchitotriose
-
-
-
-
?
4-methylumbelliferyl beta-D-N,N',N''-triacetylchitotrioside + H2O
4-methylumbelliferol + N,N',N''-triacetylchitotriose
-
-
-
?
4-methylumbelliferyl beta-D-N,N',N''-triacetylchitotrioside + H2O
4-methylumbelliferone + beta-D-N,N',N''-triacetylchitotriose
-
-
-
-
?
4-methylumbelliferyl beta-N,N',N''-triacetylchitotrioside + H2O
4-methylumbelliferol + beta-N,N',N''-triacetylchitotriose
4-methylumbelliferyl beta-N,N'-diacetylchitobioside + H2O
4-methylumbelliferol + beta-N,N'-diacetylchitobiose
4-methylumbelliferyl beta-N,N'-diacetylchitobioside + H2O
4-methylumbelliferol + N,N'-diacetylchitobiose
4-methylumbelliferyl beta-N-acetyl-D-glucosamine + H2O
4-methylumbelliferol + beta-N-acetyl-D-glucosamine
-
-
-
?
4-methylumbelliferyl GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
4-methylumbelliferone + GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
4-methylumbelliferyl N,N',N''-beta-D-triacetylchitotrioside + H2O
4-methylumbelliferol + N,N',N''-beta-D-triacetylchitotriose
substrate is prefered over shorter GlcNAc-substrates
-
-
?
4-methylumbelliferyl N,N',N''-triacetylchitotriose + H2O
4-methylumbelliferone + N,N',N''-triacetylchitotriose
4-methylumbelliferyl N,N'-diacetylchitotriose + H2O
?
-
-
-
-
?
4-methylumbelliferyl-beta-D-N,N',N''-triacetyl-chitotriose + H2O
4-methylumbelliferol + beta-D-N,N',N''-triacetyl-chitotriose
4-methylumbelliferyl-beta-D-N,N'-diacetylchitobiose + H2O
4-methylumbelliferone + N,N'-diacetylchitobiose
4-methylumbelliferyl-beta-D-N,N'-diacetylchitobioside + H2O
4-methylumbelliferone + N,N'-diacetylchitobiose
4-methylumbelliferyl-D-N,N'-diacetylchito-bioside + H2O
4-methylumbelliferone + D-N,N'-diacetylchito-bioside
-
-
-
-
?
4-nitrophenyl beta-D-GlcNAc + H2O
4-nitrophenol + N-acetyl-D-glucosamine
-
0.8% of the activity with 4-nitrophenyl-(beta-D-GlcNAc)3
-
-
?
4-nitrophenyl beta-N,N',N'',N'''-tetraacetylchitotetraoside + 3 H2O
4-nitrophenol + 2 N,N'-diacetylchitobiose
-
-
-
-
?
4-nitrophenyl beta-N,N',N'',N'''-tetraacetylchitotetraoside + H2O
4-nitrophenol + beta-N,N',N'',N'''-tetraacetylchitotetraose
-
-
-
?
4-nitrophenyl beta-N,N',N''-triacetylchitotrioside + H2O
4-nitrophenol + beta-N,N',N''-triacetylchitotriose
-
-
-
?
4-nitrophenyl beta-N,N',N''-triacetylchitotrioside + H2O
4-nitrophenol + N,N',N''-triacetylchitotriose
4-nitrophenyl beta-N,N'-diacetylchitobioside + H2O
4-nitrophenol + beta-N,N'-diacetylchitobiose
-
-
-
?
4-nitrophenyl beta-N,N'-diacetylchitobioside + H2O
4-nitrophenol + N,N'-diacetylchitobiose
4-nitrophenyl N,N'-diacetyl-beta-D-chitobioside + H2O
4-nitrophenol + N,N'-diacetyl-beta-D-chitobiose
4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
4-nitrophenol + N-acetyl-beta-D-glucosamine
4-nitrophenyl N-acetyl-beta-D-glucosaminide + H2O
4-nitrophenol + N-acetyl-beta-D-glucosamine
4-nitrophenyl N-acetylchitobioside + H2O
4-nitrophenol + N-acetylchitobiose
-
-
-
-
?
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose + H2O
4-nitrophenol + beta-1,4-N,N'-diacetyl-chitobiose
-
-
-
?
4-nitrophenyl-beta-N,N'-diacetylchitobioside + H2O
?
essential role of the two carboxylic acid residues E172 and D170 in the catalytic mechanism of Chit42
-
-
?
4-nitrophenyl-GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
4-nitrophenol + GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
-
-
-
-
?
alpha-type chitosan + H2O
?
-
98% deacetylated, 18% of the activity with colloidal chitin
-
-
?
beta-type chitin + H2O
?
-
best substrate, 148% of the activity with colloidal chitin
-
-
?
beta-type chitosan + H2O
?
-
98% deacetylated, 26% of the activity with colloidal chitin
-
-
?
chitin + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose + N-acetylglucosamine
chitin + H2O
N,N-diacetylchitobiose + N-acetylD-glucosamine
-
-
-
?
chitin oligosaccharides + H2O
N-acetyl glucosamine
glycol chitin assay method, (GlcNAc)1-6
-
-
?
chitohexaose + H2O
2 N-acetylglucosamine + 2 N,N'-diacetylchitobiose
reaction via trimer formation
-
-
?
chitohexaose + H2O
chitotetraose + chitobiose
-
the enzyme hydrolyzed the fourth glycosidic linkage from the non-reducing end of (GlcNAc)6
-
-
?
chitopentaose + H2O
N-acetylglucosamine + 2 N,N'-diacetylchitobiose
reaction via trimer formation
-
-
?
chitosan + H2O
glucosamine + chitobiose + chitooligomers with a chain length longer than 6
-
-
-
-
?
colloidal chitin + H2O
chitobiose + D-glucosamine
from crab shell
-
-
?
colloidal chitin + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose + N,N',N'',N'''-tetraacetylchitotetraose
colloidal chitin + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose + N-acetyl D-glucosamine
-
-
-
-
?
crab shell chitin + H2O
?
the enzyme cleaves internal beta-1,4 glycosidic linkages in chitooligosaccharides randomly
-
-
?
crystalline alpha-chitin + H2O
GlcNAcbeta(1-4)GlcNAcbeta + GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)-GlcNAc + GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta + GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
-
-
-
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + GlcNAcbeta(1-4)GlcNAcbeta
-
-
-
-
?
GlcNACbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
2 GlcNACbeta(1-4)GlcNAcbeta
-
-
some (GlcNAc)3 is produced through transglycosylation reaction
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + GlcNAcbeta(1-4)GlcNAc
-
i.e. (GlcNAc)6
-
-
?
GlcNACbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
GlcNACbeta(1-4)GlcNAcbeta(1-4)GlcNAc + GlcNACbeta(1-4)GlcNAcbeta
-
-
-
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
2 GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + GlcNAcbeta(1-4)GlcNAcbeta + GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
-
i.e. (GlcNAc)6
-
-
?
GlcNACbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNACbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
GlcNACbeta(1-4)GlcNAcbeta(1-4)GlcNAc + GlcNACbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + GlcNACbeta(1-4)GlcNAcbeta
-
-
product distribution is (GlcNAc)3 >(GlcNAc)4 > (GlcNAc)2 for the wild type enzyme. Some (GlcNAc)5 is produced, without formation of GlcNAc, suggesting that it is not directly produced from the initial substrate (GlcNAc)6 but produced through transglycosylation reaction
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
?
glycol chitin + H2O
N,N'-diacetylchitobiose + GlcNAc
-
exochitinase activity that yields p-nitrophenyl beta-D-N',N'',N'''-triacetylchitotriose, and then when the p-nitrophenyl beta-D-N',N'',N'''-triacetylchitotriose is accumulated, the p-nitrophenyl beta-D-N',N'',N'''-triacetylchitotriose is further cleaved into N,N'-diacetylchitobiose and GlcNAc
-
-
?
glycol chitin + H2O
N,N'-diactylchitobiose + N,N',N''-triacetylchitotriose + N,N',N'',N'''-tetraacetylchitotetraose
-
-
-
-
?
N,N',N'',N''', N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose
N,N',N'',N''', N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose + N,N',N'',N'''-tetraacetylchitotetraose
-
-
a mixture of the alpha- and beta-anomers, alpha-anomers are more dominant. BcChi-A catalyzes an anomer inversion reaction
-
?
N,N',N'',N''', N'''',N'''''-hexaacetylchitohexaose + H2O
N-acetyl-D-glucosamine + N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose + N,N',N'',N'''-tetraacetylchitotetraose
-
the enzyme hydrolyzes the third and fourth glycosidic linkages from the non-reducing end of N,N',N'',N''', N'''',N'''''-hexaacetylchitohexaose
-
-
?
N,N',N'',N''', N''''-pentaacetylchitopentaose + H2O
5 N-acetyl-D-glucosamine
-
-
-
?
N,N',N'',N''',N'''',N''''',N''''''-heptaacetylchitoheptaose + H2O
?
-
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N''',N''''-pentaacetylchitopentaose
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose
-
wild-type enzyme: the alpha/beta ratios of N,N'-diacetylchitobiose and N,N',N'',N'''-tetraacetylchitotetraose are 26.8 and 2.95, respectively
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose + N,N',N''-triacetylchitotriose
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
-
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N-acetyl-D-glucosamine
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N-acetyl-D-glucosamine + N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
-
-
the major product for GAC1 is the dimer, GAC2 produced the dimer and trimer in an equal quantity
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
(GlcNAc)2 + (GlcNAc)3
-
-
a mixture of the alpha- and beta-anomers, alpha-anomers are more dominant
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N',N''-triacetylchitotriose + N,N'-diacetylchitobiose
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N-acetyl-D-glucosamine
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N-acetyl-D-glucosamine + N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
-
-
major product
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N-acetylglucosamine + N,N'-diacetylchitobiose
reaction via trimer formation
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
4 N-acetyl-beta-D-glucosamine
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?