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Information on EC 3.2.1.14 - chitinase and Organism(s) Bacillus licheniformis and UniProt Accession Q1EM71
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3.2.1.14 chitinaseIUBMB Comments
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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Word Map
- 3.2.1.14
-
biocontrol
-
colloidal
- trichoderma
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chitin-binding
- fusarium
-
pathogenesis-related
- serratia
- n-acetylglucosamine
- marcescens
- chitosan
-
3-like
-
chi3l1
- solani
-
freezing
- gaucher
- glcnac
- beta-1,3-glucanase
-
phytopathogenic
- cellulase
- rhizoctonia
- oxysporum
- cinerea
- botrytis
- glucanase
- harzianum
- mycelial
- cuticle
-
defense-related
-
hysteresis
-
rhizosphere
- colletotrichum
- chitooligosaccharides
-
molt
- n-acetyl-d-glucosamine
- alternaria
- flounder
- circulans
- chitosanase
-
entomopathogenic
-
recrystallization
- sclerotiorum
-
transglycosylation
- viride
- beauveria
- bassiana
- pythium
- nucleopolyhedrovirus
-
anthracnose
- glucocerebrosidase
- gloeosporioides
- environmental protection
- molecular biology
- analysis
- synthesis
- pharmacology
- industry
- degradation
- medicine
- biotechnology
- agriculture
The taxonomic range for the selected organisms is: Bacillus licheniformis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
chitinase, chitotriosidase, endochitinase, antifreeze protein, chit1, amcase, chitinase a, exochitinase, acidic mammalian chitinase, class i chitinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-poly-N-acetylglucosaminidase
-
-
-
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beta-1,4-poly-N-acetyl glucosamidinase
-
-
-
-
CF-AG
-
-
-
-
CF-antigen
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-
-
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CHI-26
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-
-
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CHIT 1A
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-
-
-
CHIT 1B
-
-
-
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chitodextrinase-N-
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-
-
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Complement-fixation antigen
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-
-
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endochitinase
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-
-
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MF1 antigen
-
-
-
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poly-beta-glucosaminidase
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-
-
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UDA
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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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.
CAS REGISTRY NUMBER
COMMENTARY
9001-06-3
-
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
4-methylumbelliferyl beta-N,N'-diacetylchitobioside + H2O
4-methylumbelliferol + beta-N,N'-diacetylchitobiose
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-
-
?
4-nitrophenyl beta-N,N'-diacetylchitobioside + H2O
4-nitrophenol + N,N'-diacetylchitobiose
chitohexaose + H2O
chitobiose + ?
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-
enzyme deletion mutant rapidly hydrolyses chitohexaose and chitotetraose to chitobiose compared to chimera which hydrolyses chitohexaose and chitotetraose to chitotriose and chitobiose
-
?
chitotetraose + H2O
2 chitobiose
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enzyme deletion mutant rapidly hydrolyses chitohexaose and chitotetraose to chitobiose compared to chimera which hydrolyses chitohexaose and chitotetraose to chitotriose and chitobiose
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?
colloidal chitin + H2O
N-acetyl-D-glucosamine + N,N'-diacetylchitobiose
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-
-
?
N,N'-diacetylchitobiose + H2O
deacetylated chitooligosaccharides + acetate
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-
-
?
additional information
?
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strain MY75 has the ability to inhibit the growth of Gibberella saubinetii and Aspergillus niger, two major pathogenic fungi in agriculture, and to restrain their spore germination completely, due to chitinase activity, overview
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-
?
4-nitrophenyl beta-N,N'-diacetylchitobioside + H2O
4-nitrophenol + N,N'-diacetylchitobiose
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-
-
?
4-nitrophenyl beta-N,N'-diacetylchitobioside + H2O
4-nitrophenol + N,N'-diacetylchitobiose
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?
chitin + H2O
?
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colloidal , regenerated, or partially N-acetylated chitin substrates
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-
?
chitin + H2O
?
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optimal substrate concentration is 0.6 mg and 0.4 mg enzyme per reaction mixture
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-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
strain MY75 has the ability to inhibit the growth of Gibberella saubinetii and Aspergillus niger, two major pathogenic fungi in agriculture, and to restrain their spore germination completely, due to chitinase activity, overview
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
4-methylumbelliferyl beta-N,N'-diacetylchitobioside
pH 8.0, 55°C
additional information
additional information
-
Chi72 follows the classical Michaelis-Menten kinetics
-
0.03
4-nitrophenyl beta-N,N'-diacetylchitobioside
mutant N29S/A234V/Q387R/V465A/D480N, pH 6.0, 37°C
0.03
4-nitrophenyl beta-N,N'-diacetylchitobioside
wild-type, strain DSM8785, pH 6.0, 37°C
0.06
4-nitrophenyl beta-N,N'-diacetylchitobioside
mutant N29S/A234V/Q387R/V465A/D480N, pH 3.0, 37°C
0.06
4-nitrophenyl beta-N,N'-diacetylchitobioside
wild-type, strain DSM13, pH 6.0, 37°C
0.1
4-nitrophenyl beta-N,N'-diacetylchitobioside
wild-type, strain DSM13, pH 3.0, 37°C
0.11
4-nitrophenyl beta-N,N'-diacetylchitobioside
wild-type, strain DSM8785, pH 3.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
4-nitrophenyl beta-N,N'-diacetylchitobioside
wild-type, strain DSM8785, pH 3.0, 37°C
0.17
4-nitrophenyl beta-N,N'-diacetylchitobioside
wild-type, strain DSM13, pH 3.0, 37°C
0.23
4-nitrophenyl beta-N,N'-diacetylchitobioside
mutant N29S/A234V/Q387R/V465A/D480N, pH 3.0, 37°C
0.31
4-nitrophenyl beta-N,N'-diacetylchitobioside
wild-type, strain DSM8785, pH 6.0, 37°C
0.43
4-nitrophenyl beta-N,N'-diacetylchitobioside
wild-type, strain DSM13, pH 6.0, 37°C
0.65
4-nitrophenyl beta-N,N'-diacetylchitobioside
mutant N29S/A234V/Q387R/V465A/D480N, pH 6.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.36
4-nitrophenyl-chitobiose
wild-type, strain DSM8785, pH 3.0, 37°C
1.69
4-nitrophenyl-chitobiose
wild-type, strain DSM13, pH 3.0, 37°C
4.1
4-nitrophenyl-chitobiose
mutant N29S/A234V/Q387R/V465A/D480N, pH 3.0, 37°C
7.55
4-nitrophenyl-chitobiose
wild-type, strain DSM13, pH 6.0, 37°C
10.3
4-nitrophenyl-chitobiose
wild-type, strain DSM8785, pH 6.0, 37°C
19.4
4-nitrophenyl-chitobiose
mutant N29S/A234V/Q387R/V465A/D480N, pH 6.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
evolution
the enzyme belongs to the glycosyl hydrolase family GH18
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
additional information
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N29S/A234V/Q387R/V465A/D480N
kcat/Km of the mutant chitinase is 2.7- and 2.3fold higher than the average kcat/Km of wild types at pH 3.0 and 6.0
additional information
additional information
-
construction of a deletion mutant lacking the C-terminal chitin binding domain and of a hybrid chitinase consisting of the N-terminal catalytic domain fused to cellulose binding domain from the cellobiohydrolase II gene of Trichoderma reesei. Both recombinant chitinases retain their ability to bind to glycol-chitin. The deletion mutant is more effective on colloidal chitin than the chimera. The fusion to the cdellulose binding domain improves the affinity to colloidal chitin, activity and conformational stability in the chimera when compared with the deletion mutant
additional information
-
evaluation of immobilization of the purified enzyme, best material is carboxymethyl cellulose, enzyme activity is reduced compared to the free enzyme, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
purified recombinant enzyme, stable at, over 80% activity remaining
730871
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-25°C, 20% glycerol, up to one year with more than 80% residual activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 11.5fold from strain SK-1 by colloidal chitin affinity and anion exchange chromatography
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native enzyme from culture supernatant by ammonium sulfate fractionation, and acetone and ethanol precipitations, followed by gel filtration
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recombinant His-tagged enzyme from Lactobacillus plantarum strain WCFS1 by immobilized metal affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene chi, cloning in Escherichia coli strain NEB 5alpha, recombinant expression of His-tagged enzyme in Lactobacillus plantarum strain WCFS1 using inducible lactobacillal expression vectors pSIP403 and pSIP409, derived from the sakacin-P operon of Lactobacillus sakei
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
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the enzyme is a good candidate for application in bio-control of fungal phytopathogens
biotechnology
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the enzyme is a good candidate for application in the production of protoplasts of algal cells
environmental protection
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the enzyme is a good candidate for application in bioremedation of chitin wastes
synthesis
recombinant enzyme produced in Escherichia coli can efficiently convert colloidal chitin to N-acetyl glucosamine and chitobiose at pH 4.0, 6.0 and 9.0 at 50°C and retains its activity up to 3 days under these conditions
additional information
-
the enzyme is a good candidate for application in different biotechnological fields
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kudan, S.; Pichyangkura, R.
Purification and characterization of thermostable chitinase from Bacillus licheniformis SK-1
Appl. Biochem. Biotechnol.
157
23-35
2009
Bacillus licheniformis, Bacillus licheniformis SK-1
Xiao, L.; Xie, C.C.; Cai, J.; Lin, Z.J.; Chen, Y.H.
Identification and characterization of a chitinase-produced Bacillus showing significant antifungal activity
Curr. Microbiol.
58
528-533
2009
Bacillus licheniformis, Bacillus licheniformis MY75
Islam, S.A.; Cho, K.M.; Hong, S.J.; Math, R.K.; Kim, J.M.; Yun, M.G.; Cho, J.J.; Heo, J.Y.; Lee, Y.H.; Kim, H.; Yun, H.D.
Chitinase of Bacillus licheniformis from oyster shell as a probe to detect chitin in marine shells
Appl. Microbiol. Biotechnol.
86
119-129
2010
Bacillus licheniformis (Q1EM71), Bacillus licheniformis
Neeraja, C.; Moerschbacher, B.; Podile, A.R.
Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13
Biores. Technol.
101
3635-3641
2010
Bacillus licheniformis, Bacillus licheniformis DSM 13
Songsiriritthigul, C.; Lapboonrueng, S.; Pechsrichuang, P.; Pesatcha, P.; Yamabhai, M.
Expression and characterization of Bacillus licheniformis chitinase (ChiA), suitable for bioconversion of chitin waste
Biores. Technol.
101
4096-4103
2010
Bacillus licheniformis (B7UB89), Bacillus licheniformis, Bacillus licheniformis DSM 8785 (B7UB89)
Songsiriritthigul, C.; Pesatcha, P.; Eijsink, V.G.; Yamabhai, M.
Directed evolution of a Bacillus chitinase
Biotechnol. J.
4
501-509
2009
Bacillus licheniformis (B7UB89), Bacillus licheniformis
Youssef, A.; El-Sherif, M.; Hassan, M.; Hassan, H.; El-Aassar, S.
Purification and properties of chitinase enzyme produced by Bacillus licheniformis
J. Pure Appl. Microbiol.
7
179-188
2013
Bacillus licheniformis
-
Nguyen, H.; Nguyen, T.; Nguyen, T.; Peterbauer, C.; Mathiesen, G.; Haltrich, D.
Chitinase from Bacillus licheniformis DSM13: expression in Lactobacillus plantarum WCFS1 and biochemical characterisation
Protein Expr. Purif.
81
166-174
2012
Bacillus licheniformis (A5A699), Bacillus licheniformis DSM 13 (A5A699)
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