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Information on EC 3.2.1.14 - chitinase

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.14 chitinase
IUBMB 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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UNIPROT: Q2I0I7
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
chitinase, chitotriosidase, endochitinase, antifreeze protein, chit1, amcase, chitinase a, exochitinase, acidic mammalian chitinase, class i chitinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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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CHI-26
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CHIT 1A
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CHIT 1B
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
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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 hide
9001-06-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform ChiS
UniProt
Manually annotated by BRENDA team
isoform ChiS
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q2I0I7_9BACI
596
0
66027
TrEMBL
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Arabidopsis thaliana
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
expression of Bacillus pumilus SG2 chitinase gene and its truncated form lacking chitin binding and fibronectin type III domains in Arabidopsis thaliana plants. The two enzyme forms show almost equal hydrolytic activity toward colloidal chitin. Recombinant enzyme in plant protein extracts displays a high inhibitory effect on spore germination and radial growth of hyphae in Alternaria brassicicola, Fusarium graminearum and Botrytis cinerea, while the activity of the truncated enzyme is strongly abolished
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dehestani, A.; Kazemitabar, K.; Ahmadian, G.; Jelodar, N.B.; Salmanian, A.H.; Seyedi, M.; Rahimian, H.; Ghasemi, S.
Chitinolytic and antifungal activity of a Bacillus pumilus chitinase expressed in Arabidopsis
Biotechnol. Lett.
32
539-546
2010
Bacillus pumilus (Q2I0I7), Bacillus pumilus, Bacillus pumilus SG2 (Q2I0I7), Bacillus pumilus SG2
Manually annotated by BRENDA team