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Information on EC 3.2.1.14 - chitinase and Organism(s) Hordeum vulgare and UniProt Accession Q42839
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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: Hordeum vulgare
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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-
-
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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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chitodextrinase-N-
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-
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Complement-fixation antigen
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-
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endochitinase
MF1 antigen
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-
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poly-beta-glucosaminidase
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UDA
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-
-
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additional information
the endochitinase belongs to the glycosyl hydrolase family 19
endochitinase
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-
-
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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
chitin + H2O
?
a flexible loop controlling the enzymatic activity and specificity in the glycosyl hydrolase family 19 endochitinase from barley seeds
-
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + GlcNAcbeta(1-4)GlcNAcbeta
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-
-
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
?
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-
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?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
2 GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
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major product, plus some (GlcNAc)2 and (GlcNAc)4
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?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
?
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-
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?
additional information
?
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the class I chitinase inhibits the growth of Penicillium roquefortii, overview
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?
additional information
?
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the class I chitinase inhibits the growth of Penicillium roquefortii, overview
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?
additional information
?
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the class I chitinase inhibits the growth of Penicillium roquefortii, overview
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?
additional information
?
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purified chitinase exerts broad-spectrum antifungal activity against Botrytis cinerea (blight of tobacco), Pestalotia theae (leaf spot of tea), Bipolaris oryzae (brown spot of rice), Alternaria sp. (grain discoloration of rice), Curvularia lunata (leaf spot of clover) and Rhizoctonia solani (sheath blight of rice)
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-
?
additional information
?
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purified chitinase exerts broad-spectrum antifungal activity against Botrytis cinerea (blight of tobacco), Pestalotia theae (leaf spot of tea), Bipolaris oryzae (brown spot of rice), Alternaria sp. (grain discoloration of rice), Curvularia lunata (leaf spot of clover) and Rhizoctonia solani (sheath blight of rice)
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-
?
additional information
?
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the class I chitinase inhibits the growth of Penicillium roquefortii, overview
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-
?
additional information
?
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the class I chitinase inhibits the growth of Penicillium roquefortii, overview
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?
additional information
?
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the class I chitinase inhibits the growth of Penicillium roquefortii, overview
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?
additional information
?
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no substrate: (GlcNAc)4, (GlcNAc)3, and (GlcNAc)2
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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
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
?
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the class I chitinase inhibits the growth of Penicillium roquefortii, overview
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
no activity of mutant W72A/W82A with substrate GlcNAc hexasaccharide
additional information
-
no activity of mutant W72A/W82A with substrate GlcNAc hexasaccharide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE 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
-
chitinases are components of plant defence against higher concentrations of heavy metals. Accumulation of some isoforms in response to one but not to other metal ions suggests that these enzymes might also be involved in a more metal specific mechanism in affected plants
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). Q42839_HORVU
332
1
35370
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
molecular dynamics simulations of wild-type and mutant enzymes, overview
additional information
-
molecular dynamics simulations of wild-type and mutant enzymes, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E67Q
W72A
the mutation affects the thermal stability and specific activities toward glycol chitin and chitin hexasaccharide compared to the wild-type enzyme
W72A/W82A
the double mutation affects the thermal stability and specific activities toward glycol chitin and chitin hexasaccharide compared to the wild-type enzyme, but the effect lies between the affection of the individual mutations
W82A
the mutation affects the thermal stability and specific activities toward glycol chitin and chitin hexasaccharide compared to the wild-type enzyme
E67Q
-
loss of the enzymatic activity in E67Q is caused by a point mutation of Glu67 but not due to partial unfolding of the mutated enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of the class II chitinase with type I ribosome inactivating protein in Brassica juncea via Agrobacterium tumefaciens strain EHA105-mediated transformation. The expression of chitinase and type I ribosome inactivating protein from a heterologous source in Brassica juncea provide subsequent protection against Alternaria leaf spot disease, phenotype, overview
overexpression in Escherichia coli. Since the protein is produced as insoluble inclusion bodies, the protein is solubilized and refolded
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
due to the potential of broad-spectrum antifungal activity barley chitinase gene can be used to enhance fungal-resistance in crop plants such as rice, tobacco, tea and clover
additional information
the expression of chitinase and type I ribosome inactivating protein from a heterologous source in Brassica juncea provide subsequent protection against Alternaria leaf spot disease and can be helpful in increasing the production of Indian mustard
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leah, R.; Tommerup, H.; Svendsen, I.; Mundy, J.
Biochemical and molecular characterization of three barley seed proteins with antifungal properties
J. Biol. Chem.
266
1564-1573
1991
Hordeum vulgare
Andersen, M.D.; Jensen, A.; Robertus, J.D.; Leah, R.; Skriver, K.
Heterologous expression and characterization of wild-type and mutant forms of a 26 kDa endochitinase from barley (Hordeum vulgare L.)
Biochem. J.
322
815-822
1997
Hordeum vulgare
-
Bekesiova, B.; Hraska, S.; Libantova, J.; Moravcikova, J.; Matusikova, I.
Heavy-metal stress induced accumulation of chitinase isoforms in plants
Mol. Biol. Rep.
35
579-588
2008
Vicia faba, Glycine max, Hordeum vulgare, Pisum sativum, Zea mays
Kirubakaran, S.I.; Sakthivel, N.
Cloning and overexpression of antifungal barley chitinase gene in Escherichia coli
Protein Expr. Purif.
52
159-166
2007
Hordeum vulgare (P11955), Hordeum vulgare
Fukamizo, T.; Miyake, R.; Tamura, A.; Ohnuma, T.; Skriver, K.; Pursiainen, N.V.; Juffer, A.H.
A flexible loop controlling the enzymatic activity and specificity in a glycosyl hydrolase family 19 endochitinase from barley seeds (Hordeum vulgare L.)
Biochim. Biophys. Acta
1794
1159-1167
2009
Hordeum vulgare (P23951), Hordeum vulgare
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
Dennhart, N.; Weigang, L.M.; Fujiwara, M.; Fukamizo, T.; Skriver, K.; Letzel, T.
26kDa endochitinase from barley seeds: real-time monitoring of the enzymatic reaction and substrate binding experiments using electrospray ionization mass spectrometry
J. Biotechnol.
143
274-283
2009
Hordeum vulgare
Chhikara, S.; Chaudhury, D.; Dhankher, O.; Jaiwal, P.
Combined expression of a barley class II chitinase and type I ribosome inactivating protein in transgenic Brassica juncea provides protection against Alternaria brassicae
Plant Cell Tissue Organ Cult.
83-89
83-89
2012
Hordeum vulgare (P23951)
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