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Information on EC 3.2.1.14 - chitinase and Organism(s) Moritella marina and UniProt Accession B1VBB0
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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: Moritella marina
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
-
-
-
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CF-antigen
-
-
-
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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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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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-
-
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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
4-nitrophenyl beta-1,4-N,N'-diacetyl-chitobiose + H2O
4-nitrophenol + beta-1,4-N,N'-diacetyl-chitobiose
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-
-
?
chitin + H2O
?
chitinases hydrolyse the beta-1,4-linkages in chitin
-
-
?
additional information
?
-
the enzyme is not active with synthetic 4-nitrophenyl-linked glycosidic substrates, overview
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-
?
additional information
?
-
-
the enzyme is not active with synthetic 4-nitrophenyl-linked glycosidic substrates, 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
chitin + H2O
?
chitinases hydrolyse the beta-1,4-linkages in chitin
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme is not affected by various bivalent cations
additional information
-
the enzyme is not affected by various bivalent cations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme is not affected by various bivalent cations and EDTA, DTT, iodoacetic acid, and PMSF
-
additional information
-
the enzyme is not affected by various bivalent cations and EDTA, DTT, iodoacetic acid, and PMSF
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme is not affected by various bivalent cations and EDTA, DTT, iodoacetic acid, and PMSF
-
additional information
-
the enzyme is not affected by various bivalent cations and EDTA, DTT, iodoacetic acid, and PMSF
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.101
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 0°C, purified recombinant enzyme
0.37
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 10°C, purified recombinant enzyme
0.416
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 15°C, purified recombinant enzyme
0.5
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 5°C or 20°C, purified recombinant enzyme
0.555
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 28°C, purified recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.79
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 0°C, purified recombinant enzyme
4.33
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 5°C, purified recombinant enzyme
5.46
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 10°C, purified recombinant enzyme
7.33
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 15°C, purified recombinant enzyme
11.88
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 20°C, purified recombinant enzyme
19.54
4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
pH 5.0, 28°C, purified recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.91
purified recombinant enzyme, substrate 4-nitrophenyl-beta-1,4-N,N'-diacetyl-chitobiose
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
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3
purified recombinant enzyme, 3 days, loss of 80% of activity at 4°C
692256
4 - 10
the purified recombinant Chi60 exhibits broad pH stability maintaining over 60% activity after 10 days at a pH range at 4°C
692256
8 - 10
purified recombinant enzyme, 10 days, no loss of activity at 4°C
692256
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme stability at 18°C and 28°C is similar to the stability at 4°C
additional information
-
the enzyme stability at 18°C and 28°C is similar to the stability at 4°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene chi60, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
EXTERNAL LINKS (specific for EC-Number 3.2.1.14)
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Release 2023.1 (January 2023)
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