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Information on EC 3.2.1.14 - chitinase and Organism(s) Secale cereale and UniProt Accession Q9FRV1
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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
-
3-like
-
chi3l1
- solani
-
freezing
- gaucher
- glcnac
- beta-1,3-glucanase
-
phytopathogenic
- cellulase
- rhizoctonia
- oxysporum
- cinerea
- botrytis
- glucanase
- harzianum
- mycelial
- cuticle
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defense-related
-
hysteresis
-
rhizosphere
- colletotrichum
- chitooligosaccharides
-
molt
- n-acetyl-d-glucosamine
- alternaria
- flounder
- circulans
- chitosanase
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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: Secale cereale
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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-
-
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beta-1,4-poly-N-acetyl glucosamidinase
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-
-
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CF-AG
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-
-
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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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-
-
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CHIT 1B
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-
-
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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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-
-
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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
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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
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
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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). CHIA_SECCE
321
0
33642
Swiss-Prot
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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