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Information on EC 3.2.1.14 - chitinase and Organism(s) Oryza sativa and UniProt Accession P24626
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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
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biocontrol
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colloidal
- trichoderma
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chitin-binding
- fusarium
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pathogenesis-related
- serratia
- n-acetylglucosamine
- marcescens
- chitosan
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3-like
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chi3l1
- solani
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freezing
- gaucher
- glcnac
- beta-1,3-glucanase
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phytopathogenic
- cellulase
- rhizoctonia
- oxysporum
- cinerea
- botrytis
- glucanase
- harzianum
- mycelial
- cuticle
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defense-related
-
hysteresis
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rhizosphere
- colletotrichum
- chitooligosaccharides
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molt
- n-acetyl-d-glucosamine
- alternaria
- flounder
- circulans
- chitosanase
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entomopathogenic
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recrystallization
- sclerotiorum
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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: Oryza sativa
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
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CF-AG
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CF-antigen
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-
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CHI-26
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CHIT 1A
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CHIT 1B
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-
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chitodextrinase-N-
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Complement-fixation antigen
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endochitinase
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MF1 antigen
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poly-beta-glucosaminidase
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UDA
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additional information
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OsChia1b is a class I chitinase of glucohydrolase family 19
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
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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
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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
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
?
-
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose
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wild-type enzyme: the alpha/beta ratios of N,N'-diacetylchitobiose and N,N',N'',N'''-tetraacetylchitotetraose are 26.8 and 2.95, respectively
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-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose + N,N',N''-triacetylchitotriose
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OsChia1c almost exclusively generates (GlcNAc)3 and small amounts of (GlcNAc)2 and (GlcNAc)4, OsChia2b hydrolyzes the substrate to predominantely yield (GlcNAc)2
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?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
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-
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
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poorly hydrolyzed by OsChia1c but efficiently hydrolyzed by OsChia2b to predominantely yield (GlcNAc)2
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-
?
N,N',N''-triacetylchitotriose + H2O
N-acetyl-D-glucosamine + N,N'-diacetylchitobiose
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OsChia2b
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?
chitin + H2O
?
chitin from fungal cell wall, the chitinase exhibits different antifungal activities against the four fungi, which is directly correlated to the surface microstructure and the proportion of chitin in the fungal cell wall, antifungal mechanism of action of chitinase against four plant pathogenic fungi, i.e. Rhizopus stolonifer, Botrytis squamosa, Pythium aphanidermatum, and Aspergillus niger, overview
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-
?
chitin + H2O
?
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chitinase is a glycoside hydrolase that catalyzes the degradation of chitin
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?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
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-
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?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
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poorly hydrolyzed by OsChia1c but efficiently hydrolyzed by OsChia2b to predominantely yield (GlcNAc)2
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?
partially N-acetylated chitosan + H2O
?
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for the class I enzyme OsChia1cDELTAChBD, the reducing end residue is preferentially acetylated, although the specificity is not absolute. The nearest neighbor to the acetylated reducing end residue is specifically acetylated. The nonreducing end residue produced by the class I enzyme is exclusively acetylated, although there is a low but significant preference for deacetylated units at the nearest neighbor to the nonreducing end. The three contiguous subsites (-2), (-1), and (+1) of the class I enzyme are specific to three consecutive GlcNAc residues of the substrate
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?
partially N-acetylated chitosan + H2O
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the reducing end residue of the enzymatic products obtained by the class III enzyme OsChib1a is exclusively acetylated, whereas both acetylated and deacetylated units are found at the nearest neighbor to the reducing end residue. Both acetylated and deacetylated units are also found at the nonreducing end residue and its nearest neighbor of the class III enzyme products. Only subsite (-1) among the contiguous subsites (-2) to (+2) of the class III enzyme is specific to an acetylated residue
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?
additional information
?
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the class III enzyme OsChib1a might act toward an endogenous complex carbohydrate containing GlcNAc residue
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?
additional information
?
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the target of the class I enzyme OsChia1cDELTAChBD might be a consecutive GlcNAc sequence probably in the cell wall of fungal pathogen
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?
additional information
?
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OsChia1b shows no activity against N-acetylchitotriose, and crystalline beta-chitin is a poor substrate. OsChia1b substrate binding specificity depends on the N-acetyl groups of the substrate. About 80% of added OsChia1b binds to colloidal chitin, whereas less than 30% of added OsChia1b binds to chitosan 7B, with 70% deacetylated chitin, avicel, and acid-swollen cellulose, less than 10% of OsChia1b binds to beta-1,3-glucan, curdlan
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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
chitin + H2O
?
chitin from fungal cell wall, the chitinase exhibits different antifungal activities against the four fungi, which is directly correlated to the surface microstructure and the proportion of chitin in the fungal cell wall, antifungal mechanism of action of chitinase against four plant pathogenic fungi, i.e. Rhizopus stolonifer, Botrytis squamosa, Pythium aphanidermatum, and Aspergillus niger, overview
-
-
?
chitin + H2O
?
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chitinase is a glycoside hydrolase that catalyzes the degradation of chitin
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-
?
additional information
?
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-
the class III enzyme OsChib1a might act toward an endogenous complex carbohydrate containing GlcNAc residue
-
-
?
additional information
?
-
-
the target of the class I enzyme OsChia1cDELTAChBD might be a consecutive GlcNAc sequence probably in the cell wall of fungal pathogen
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
KM: 1.36 mg/ml with chitin as substrate
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additional information
additional information
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OsChia1c: 0.9 mg/ml with colloidal chitin as substrate and 0.4 mg/ml with glycol chitin as substrate, OsChia1cDELTACBD: 1.2 mg/ml with colloidal chitin as substrate and 0.2 mg/ml with glycol chitin as substrate, OsChia2b: 1.9 mg/ml with colloidal chitin as substrate and 0.4 mg/ml with glycol chitin as substrate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
254
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purified OsChia1b, substrate GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAc
additional information
additional information
purified recombinant enzyme, and antifungal activities, overview
additional information
-
purified recombinant enzyme, and antifungal activities, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
OsChia1cDELTACBD
W159A
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mutation increases hydrolytic activity toward N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose and toward polysaccharide substrates. Similar results are obtained for kcat/Km value determined for substrate reduced N-acetylchitopentaose. The mutation shifts the splitting positions in N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose to the reducing end side
additional information
-
the loop II deletion and the W159A mutation increases hydrolytic activity toward N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose and toward polysaccharide substrates. Similar results are obtained for kcat/Km values determined for substrate reduced N-acetylchitopentaose. The two mutations shift the splitting positions in N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose to the reducing end side, but the shift is less intensive in the Trp mutant
OsChia1cDELTACBD
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truncated chitin-binding domain mutant, no changes in activity towards chitohexaose compared with wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant OsChia1b from Escherichia coli by ammonium sulfate fractionation and chitin affinity chromatography to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloning in Escherichia coli strain DH5alpha, expression in Pichia pastoris strain GS115
expression of a clone named RCB4l, that encodes the N-terminal and internal amino acid sequence, in Escherichia coli
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expression of wild-type OsChia1b and the two mutant chitinases, loop II-deletion mutant (OsChia1bDELTAloopII) and W159A mutant (OsChia1bW159A) in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, Y.I.; Baek, J.M.; Park, H.Y.; Choi, Y.D.; Kim, S.I.
Isolation and characterization of cDNA clones encoding class I chitinase in suspension cultures of rice cell
Biosci. Biotechnol. Biochem.
58
1164-1166
1994
Oryza sativa
Truong, N.H.; Park, S.M.; Nishizawa, Y.; Watanabe, T.; Sasaki, T.; Itoh, Y.
Structure, heterologous expression, and properties of rice (Oryza sativa L.) family 19 chitinases
Biosci. Biotechnol. Biochem.
67
1063-1070
2003
Oryza sativa
Baek, J.H.; Han, B.K.; Jo, D.H.
Distribution of chitinases in rice (Oryza sativa L) seed and characterization of a hull-specific chitinase
J. Biochem. Mol. Biol.
34
310-315
2001
Oryza sativa
-
Park, H.Y.; Pan, C.H.; So, M.Y.; Ah, J.H.; Jo, D.H.; Kim, S.I.
Purification, characterization, and cDNA cloning of rice class III chitinase
Mol. Cells
13
69-76
2002
Oryza sativa
Sasaki, C.; Itoh, Y.; Takehara, H.; Kuhara, S.; Fukamizo, T.
Family 19 chitinase from rice (Oryza sativa L.): substrate-binding subsites demonstrated by kinetic and molecular modeling studies
Plant Mol. Biol.
52
43-52
2003
Oryza sativa
Sasaki, C.; Varum, K.M.; Itoh, Y.; Tamoi, M.; Fukamizo, T.
Rice chitinases: sugar recognition specificities of the individual subsites
Glycobiology
16
1242-1250
2006
Oryza sativa
Mizuno, R.; Fukamizo, T.; Sugiyama, S.; Nishizawa, Y.; Kezuka, Y.; Nonaka, T.; Suzuki, K.; Watanabe, T.
Role of the loop structure of the catalytic domain in rice class I chitinase
J. Biochem.
143
487-495
2008
Oryza sativa
Mizuno, R.; Itoh, Y.; Nishizawa, Y.; Kezuka, Y.; Suzuki, K.; Nonaka, T.; Watanabe, T.
Purification and characterization of a rice class I chitinase, OsChia1b, produced in Escherichia coli
Biosci. Biotechnol. Biochem.
72
893-895
2008
Oryza sativa
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