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Information on EC 3.2.1.14 - chitinase and Organism(s) Trichoderma harzianum and UniProt Accession P48827
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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: Trichoderma harzianum
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
-
-
-
-
endochitinase
-
-
-
-
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
4-nitrophenyl beta-N,N'-diacetylchitobioside + H2O
?
essential role of the two carboxylic acid residues E172 and D170 in the catalytic mechanism of Chit42
-
-
?
4-methylumbelliferyl-beta-D-N,N'-diacetylchitobioside + H2O
4-methylumbelliferone + N,N'-diacetylchitobiose
-
chit37 and chit42
-
-
?
4-nitrophenyl beta-D-N,N',N''-triacetylchitotrioside + H2O
4-nitrophenyl beta-D-N,N'-diacetylchitobioside + 4-nitrophenyl N-acetylglucosaminide + beta-D-N,N'-diacetylchitobioside + N-acetylglucosamine
-
-
-
?
cell wall + H2O
chitin oligosaccharides
-
chit42, cell wall from Botrytis cinerea
-
-
?
chitopentaose + H2O
chitobiose + chitotriose
-
-
main product chitobiose, small amounts of chitotriose and N-acetylglucosamine also
?
N,N',N''-triacetylchitotriose + H2O
N-acetylglucosamine + N,N'-diacetylchitobiose
-
-
-
?
p-nitrophenyl-beta-D-N,N'-diacetylchitobiose + H2O
N,N'-diacetylchitobiose + p-nitrophenol
-
chit37 and chit42
-
-
?
p-nitrophenyl-beta-D-N,N'-diacetylchitobiose + H2O
p-nitrophenol + N,N'-diacetylchitobiose
-
-
-
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
colloidal chitin
chit37 and chit42 main product chitobiose, some N-acetylglucosamine and chitotriose also, chit33 main product chitotetraose, chitobiose, chitotetraose, n-acetylglucosamine also present
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
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from ground crab shell
-
-
?
additional information
?
-
essential role of E172, D170 and E145 in the catalytic mechanism of Chit33
-
-
?
additional information
?
-
essential role of E172, D170 and E145 in the catalytic mechanism of Chit33
-
-
?
additional information
?
-
-
essential role of E172, D170 and E145 in the catalytic mechanism of Chit33
-
-
?
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
allosamidin
-
binding is dependent on the E172 residue, the acid/base catalyst of isoform Chit42
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.9 - 1.1
4-nitrophenyl 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranoside
0.3152
4-nitrophenyl beta-D-N,N',N''-triacetylchitotrioside
at pH 4.0 and 50°C
additional information
additional information
-
colloidal chitin, chit33 0.3 mg/ml, chit37 0.5 mg/ml, chit42 1 mg/ml
-
0.9
4-nitrophenyl 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranoside
pH 6.5, wild-type enzyme from Trichoderma harzianum
1.1
4-nitrophenyl 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranoside
pH 6.5, wilde-type recombinant enzyme expressed in Escherichia coli
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.267 - 0.35
4-nitrophenyl 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranoside
0.107
4-nitrophenyl beta-D-N,N',N''-triacetylchitotrioside
at pH 4.0 and 50°C
0.267
4-nitrophenyl 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranoside
pH 6.5, wild-type enzyme from Trichoderma harzianum
0.35
4-nitrophenyl 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-2-deoxy-beta-D-glucopyranoside
pH 6.5, wilde-type recombinant enzyme expressed in Escherichia coli
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47
enzyme recombinantly expressed in Escherichia coli and refolded
50
50
enzyme recombinantly expressed in Escherichia coli and refolded
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23 - 50
40 - 55
40°C: about 80% of maximal activity, 55°C: about 90% of maximal activity, 65°C: no activity, enzyme form Trichoderma harzianum
40 - 60
40°C: about 70% of maximal activity, 60°C: about 80% of maximal activity, 70°C, no activity, enzyme recombinantly expressed in Escherichia coli and refolded
23 - 50
23°C: about 50% of maximal activity, 50°C: about 30% of maximal activity, enzyme form Trichoderma harzianum
23 - 50
23°C: about 60% of maximal activity, 50°C: about 30% of maximal activity, enzyme recombinantly expressed in Escherichia coli and refolded
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
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). CHI42_TRIHA
423
0
46057
Swiss-Prot
Secretory Pathway (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Chit33 does not contain any putative N-glycosylation site
additional information
Chit33 does not contain any putative N-glycosylation site
additional information
-
Chit33 does not contain any putative N-glycosylation site
additional information
Chit33 does not contain any putative N-glycosylation site
additional information
Chit33 does not contain any putative N-glycosylation site
additional information
-
Chit33 does not contain any putative N-glycosylation site
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D170A/E172Q
-
improved binding afinities toward substrates (GlcNAc)5, (GlcNAc)6, and GlcNbeta-4(GlcNAc)4
E172Q
-
mutant of isoform Chi42, catalytically inactive. The E172Q mutant binds chitinoligosaccharides, tetra-, penta- and hexamers, with an increasing affinity from 12 to 0.2 microM whereas no binding of chitinbiose, -triose or 3-sialyl-N-acetyllactosamine can be measured
E317A/E172Q
-
affinity decrease down to 20-25% of the affinity of the E172Q reference protein for substrates (GlcNAc)5, (GlcNAc)6
T133D
-
mutation alters substrate binding specificity of Chit42 toward binding of GlcNbeta-4(GlcNAc)4 by providing a counter charge at subsite -3
T133N/E172Q
-
no significant loss of affinity for any of the compounds tested, increase in the selectivity for Galbeta-4(GlcNAc)4
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chit33 1.3fold to homogeneity, chit42 8fold to homogeneity, chit37 3.4fold to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. Cytoplasmic overexpression results in inclusion body formation. Active enzyme can be recovered after refolding. Periplasmic proves to be better suited for mutagenesis purposes
expression in Escherichia coli. Cytoplasmic overexpression results in inclusion body formation. Active enzyme can be recovered after refolding. Periplasmic proves to be better suited for mutagenesis purposes
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ridout, C.J.; Coley-Smith, J.R.; Lynch, J.M.
Fractionation of extracellular enzymes from a mycoparasitic strain fo Trichoderma harzianum
Enzyme Microb. Technol.
10
180-187
1988
Trichoderma harzianum
-
De la Cruz, J.; Hidalgo-Gallego, A.; Lora, J.M.; Benitez, T.; Pintor-Toro, J.A.; Llobell, A.
Isolation and characterization of three chitinases from Trichoderma harzianum
Eur. J. Biochem.
206
859-867
1992
Trichoderma harzianum, Trichoderma harzianum CECT 2413
Boer, H.; Simolin, H.; Cottaz, S.; Soederlund, H.; Koivula, A.
Heterologous expression and site-directed mutagenesis studies of two Trichoderma harzianum chitinases, Chit33 and Chit42, in Escherichia coli
Protein Expr. Purif.
51
216-226
2007
Trichoderma harzianum (P48827), Trichoderma harzianum (Q12713), Trichoderma harzianum
Lienemann, M.; Boer, H.; Paananen, A.; Cottaz, S.; Koivula, A.
Toward understanding of carbohydrate binding and substrate specificity of a glycosyl hydrolase 18 family (GH-18) chitinase from Trichoderma harzianum
Glycobiology
19
1116-1126
2009
Trichoderma harzianum
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