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Information on EC 3.2.1.14 - chitinase and Organism(s) Triticum aestivum and UniProt Accession Q41539
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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
-
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: Triticum aestivum
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
-
-
-
-
beta-1,4-poly-N-acetyl glucosamidinase
-
-
-
-
CF-AG
-
-
-
-
CF-antigen
-
-
-
-
CHI-26
-
-
-
-
CHIT 1A
-
-
-
-
CHIT 1B
-
-
-
-
chitodextrinase-N-
-
-
-
-
Complement-fixation antigen
-
-
-
-
endochitinase
-
-
-
-
MF1 antigen
-
-
-
-
poly-beta-glucosaminidase
-
-
-
-
UDA
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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
chitosan + H2O
chitosan oligosaccharides
-
reacetylated
from diacetylchitobiose to tetraacetylchitotetraose
?
chitotetraose + H2O
N-acetylglucosamine + chitobiose + chitotriose
-
tritiated
only traces of chitotriose and N-acetylglucosamine
?
glycol chitin + H2O
N-acetylglucosamine + ?
-
tritiated and unlabeled
-
-
?
N,N',N''-triacetylchitotriose + H2O
N-acetylglucosamine + N,N'-diacetylchitobiose
-
3H labelled, only slightly attacked
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
[acetyl-3H]chitin
-
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
[acetyl-3H]chitin
chitobiose, biotriose and biotetraose from nascent chitin, higher oligosaccharides from preformed chitin
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
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
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
additional information
?
-
-
the class I chitinase inhibits the growth of Penicillium roquefortii, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14.6
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
two basic isoforms with pI values of 7.6 and 8.0
8
two basic isoforms with pI values of 7.6 and 8.0
7.6
two basic isoforms with pI values of 7.6 and 8.0
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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). Q41539_WHEAT
320
0
33602
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
-
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
determination of the primary structure by mass spectrometry, sequence comparisons, overview
additional information
-
determination of the primary structure by mass spectrometry, sequence comparisons, overview
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cabib, E.
Endochitinase from wheat germ
Methods Enzymol.
161
498-501
1988
Triticum aestivum
-
Cabib, E.
Assay for chitinase using tritiated chitin
Methods Enzymol.
161
424-426
1988
Serratia marcescens, Triticum aestivum
-
Boller, T.; Mauch, F.
Colorimetric assay for chitinase
Methods Enzymol.
161
430-435
1988
Triticum aestivum
-
Molano, J.; Polacheck, I.; Duran, A.; Cabib, E.
An endochitinase from wheat germ. Activity on nascent and preformed chitin
J. Biol. Chem.
254
4901-4907
1979
Triticum aestivum
Soerensen, H.P.; Madsen, L.S.; Petersen, J.; Andersen, J.T.; Hansen, A.M.; Beck, H.C.
Oat (Avena sativa) seed extract as an antifungal food preservative through the catalytic activity of a highly abundant class I chitinase
Appl. Biochem. Biotechnol.
160
1573-1584
2009
Hordeum vulgare (P11955), Hordeum vulgare (Q42839), Hordeum vulgare, Avena sativa (P86181), Triticum aestivum (Q41539), Triticum aestivum (Q6T484), Triticum aestivum (Q8W427), Triticum aestivum (Q8W428), Triticum aestivum (Q9XEN6), Triticum aestivum, Secale cereale (Q9AXR9), Secale cereale (Q9FRV1), Secale cereale
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