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Information on EC 3.5.1.41 - chitin deacetylase and Organism(s) Colletotrichum lindemuthianum and UniProt Accession Q6DWK3
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3.5.1.41 chitin deacetylaseIUBMB Comments
Hydrolyses the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin.
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Word Map
- 3.5.1.41
- chitosan
- deacetylases
-
colletotrichum
-
peritrophic
- lindemuthianum
- chitooligosaccharides
- rouxii
- chitosanase
-
chitin-binding
-
chitinolytic
-
n-deacetylated
-
acetamido
- synthesis
- absidia
-
peritrophin-a
-
larval-pupal
- agriculture
- medicine
- drug development
- analysis
The taxonomic range for the selected organisms is: Colletotrichum lindemuthianum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
chitin deacetylase, lmcda2, lmcda1, bmcda7, cdayj, bmcda8, chitin deacetylase 1, fv-pda, ancda, clcda, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
additional information
the enzyme belongs to the carbohydrate esterase family CE 4
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chitin + H2O = chitosan + acetate
ligand binding to the enzyme, computational docking analysis, catalytic mechanism via a tetrahedral oxyanion intermediate, and active site structure with a conserved metal-binding triad consisting of His104, His108, and Asp50
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
chitin amidohydrolase
Hydrolyses the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin.
CAS REGISTRY NUMBER
COMMENTARY
56379-60-3
-
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
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-bromoacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + bromoacetate
-
-
-
?
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-chloroacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + chloroacetate
-
-
-
?
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-fluoroacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + fluoroacetate
-
-
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNbeta(1-4)GlcNAc + acetate
-
-
-
?
glycol chitin + H2O
deacetylated glycol chitin + acetate
-
-
-
r
hexa-N-acetyl-chitohexaose + H2O
chitohexaose + acetate
-
-
-
?
N,N'-diacetylchitobiose + H2O
deacetylated chitooligosaccharides + acetate
the enzyme deacetylates the non-reducing GlcNAc of N,N'-diacetylchitobiose
-
-
r
penta-N-acetyl-chitopentaose + H2O
chitopentaose + acetate
-
-
-
?
tetra-N-acetyl-chitotetraose + H2O
chitotetraose + acetate
-
-
-
?
(N-acetyl-D-glucosamine)2 + H2O
(GlcN)GlcNAc + acetate
-
-
-
-
?
(N-acetyl-D-glucosamine)4 + H2O
(GlcN)3GlcNAc + acetate
-
-
-
-
?
(N-acetyl-D-glucosamine)5
(GlcN)4GlcNAc + acetate
-
-
-
-
?
(N-acetyl-D-glucosamine)5 + H2O
(GlcN)4GlcNAc + acetate
-
-
-
-
?
2 N,N',N'',N''',N''''-pentaacetylchitopentaose + 3 H2O
GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + 3 acetate
-
-
initial product: mixture of two isomers, no processivity
?
3 N,N',N''-triacetylchitotriose + 2 H2O
GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN + GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + 3 acetate
-
no detectable hydrolysis at low substrate concentrations i.e. 0.1 mM
initial product: mixture of three isomers
?
chitobiose + acetate
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-D-glucose + H2O
-
-
-
?
chitosan tetramer + acetate
beta-N-acetyl-D-glucosamine-(1-4)-beta-N-acetyl-D-glucosamine-(1-4)-beta-N-acetyl-D-glucosamine-(1-4)-D-glucosamine + H2O
-
-
beta-D-GlcNAc-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc-(1-4)-D-GlcN
?
chitotetraose + acetate
? + H2O
-
-
mixture of partially acetylated compounds
?
GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcNAc + acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcN-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcNAc + GlcN-beta-(1-4)-GlcNAc-beta-(1-4)-GlcN-beta-(1-4)-GlcNAc + acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + GlcN-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc + GlcNAc-beta-(1,4)-GlcN-beta-(1,4)-GlcNAc + GlcNAc-beta-(1,4)-GlcNAc-beta-(1,4)-GlcN
-
time courses for hydrolysis of the N-acetyl groups are followed spectrometrically
GlcN-beta-(1,4)-GlcNAc-beta-(1,4)-GlcNAc, GlcNAc-beta-(1,4)-GlcN-beta-(1,4)-GlcNAc and GlcNAc-beta-(1,4)-GlcNAc-beta-(1,4)-GlcN are formed in the proportions 22:50:28
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 3 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 4 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcN-beta-(1-4)-GlcNAc + acetate
-
time courses for hydrolysis of the N-acetyl groups are followed spectrometrically
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
-
time courses for hydrolysis of the N-acetyl groups are followed spectrometrically
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 5 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
acetate + ?
-
time courses for hydrolysis of the N-acetyl groups are followed spectrometrically
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 6 acetate
-
-
-
-
?
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc + H2O
GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN-beta-(1-4)-GlcN + 7 acetate
-
-
-
-
?
monoacetylated chitopentaose + H2O
chitopentaose + acetate
-
-
-
-
?
monoacetylated chitotetraose + H2O
chitotetraose + acetate
-
-
-
-
?
monoacetylated chitotriose + H2O
chitotriose + acetate
-
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + 4 H2O
3 GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc + 4 acetate
-
-
initial product: mixture of three isomers, no processivity
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
-
-
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + 5 H2O
chitopentaose + 5 acetate
-
-
end product
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
-
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + 4 H2O
chitotetraose + 4 acetate
-
-
end product
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
GlcNAc-beta-(1->4)-GlcNAc-beta-(1->4)-GlcN-beta-(1->4)-GlcNAc + acetate
-
-
after 10 min, only product, no processivity
?
p-nitrophenyl 2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranoside + acetate
p-nitrophenyl N,N'-diacetyl-beta-chitobioside + H2O
-
-
-
?
chitin + H2O
chitosan + acetate
the enzyme is an endo-chitin de-N-acetylase
-
-
?
chitin + H2O
chitosan + acetate
-
partially N-deacetylated water soluble chitin
-
?
chitin + H2O
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
high substrate concentration needed
-
-
?
N,N'-diacetylchitobiose + H2O
deacetylated chitooligosaccharides + acetate
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
deacetylated chitooligosaccharides + acetate
-
high substrate concentration needed
-
-
?
additional information
?
-
binding study of an N-acetylglucosaminyl trimer to the enzyme, computational docking
-
-
?
additional information
?
-
-
binding study of an N-acetylglucosaminyl trimer to the enzyme, computational docking
-
-
?
additional information
?
-
substrate specificity, overview, no activity with chitotriose
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with chitotriose
-
-
?
additional information
?
-
substrate recognition and specificity of the chitin deacetylase. Most CDAs are highly inactive on crystalline chitin and have a preference for soluble chitins, such as glycol-chitin or chitin oligomers, as well as partially deacetylated chitin (chitosans). The inactivity on insoluble chitin is most likely due to the inaccessibility of the acetyl groups in the tightly packed chitin structure. Some CDAs contain carbohydrate binding modules (CBM) fused to the catalytic domain that seem to increase the accessibility of the chitin chains to the catalytic domain, resulting in a (slightly) enhanced deacetylase activity. Structures of the substrates of CE4 enzymes and representative deacetylated products, overview. The enzyme from Colletotrichum lindemuthianum is able to fully deacetylate chitooligosaccharides with a DP equal to or greater than 3, while it only deacetylates the non-reducing GlcNAc of N,N'-diacetylchitobiose. This enzyme is reversible, as it is also able to catalyze the acetylation of chitosan oligomers
-
-
?
additional information
?
-
-
chitin deacetylase is not effective on natural insoluble crystalline chitin
-
-
?
additional information
?
-
-
the recombinant enzyme deacetylates the complex oligosaccharide substrates with various acetyls produced by endo-chitosanase from Aspergillus fumigatus hydrolyzing chitosan. Substrate and product identification by mass spectrometric analysis, overview. (GlcNAc)4 is fully deacetylated into (GlcN)4, and the enzyme deacetylates (GlcNAc)4 and (GlcNAc)5 much faster than (GlcNAc)3 and (GlcNAc)2. Chitotriose is also fully deacetylated through a random deacetylation process, while chitobiose (GlcNAc)2, is only deacetylated at the non-reducing GlcNAc residue. The enzyme exclusively produces Glc-NGlcNAc, and cannot deacetylate GlcNAc
-
-
?
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
chitosan + acetate
-
plain chitin is a poor substrate, but glycolated, reprecipitated or depolymerized chitins are good ones
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Zn2+
Ca2+
-
the enzyme activity of chitin deacetylase can be enhanced in the presence of Ca2+ (1 mM)
Co2+
Zn2+
-
the enzyme activity of chitin deacetylase can be enhanced in the presence of Zn2+ (1 mM)
additional information
Zn2+
tightly bound to the conserved metal-binding triad consisting of His104, His108, and Asp50, structure analysis
Co2+
-
the enzyme activity of chitin deacetylase can be enhanced in the presence of Co2+ (1 mM)
additional information
Li+ and Mn2+ have no effect on enzyme activity
additional information
-
Li+ and Mn2+ have no effect on enzyme activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
addition of EDTA eliminates total chitin deacetylase activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.102
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-bromoacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose
pH 8.5, 30°C, continuous spectrophotometric assay
0.18
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-chloroacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose
pH 8.5, 30°C, continuous spectrophotometric assay
0.14
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-fluoroacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose
pH 8.5, 30°C, continuous spectrophotometric assay
18
GlcNAcbeta(1-4)GlcNAc
pH 8.5, 30°C, continuous spectrophotometric assay
0.125
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
pH 8.5, 30°C, continuous spectrophotometric assay
1.5
hexa-N-acetyl-chitohexaose
pH 8.0, 50°C, recombinant enzyme
5.7
penta-N-acetyl-chitopentaose
pH 8.0, 50°C, recombinant enzyme
8.9
tetra-N-acetyl-chitotetraose
pH 8.0, 50°C, recombinant enzyme
0.125
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc
-
pH 8.5, 30°C
0.079
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc
-
pH 8.5, 30°C
0.048
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc
-
pH 8.5, 30°C
0.66
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
pH 8.5, 30°C, continuous spectrophotometric assay
4.3
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
pH 7.0, 37°C, fluorogenic labeling method assay
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
31
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-bromoacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose
pH 8.5, 30°C, continuous spectrophotometric assay
47
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-chloroacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose
pH 8.5, 30°C, continuous spectrophotometric assay
68
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-fluoroacetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-D-glucose
pH 8.5, 30°C, continuous spectrophotometric assay
11
GlcNAcbeta(1-4)GlcNAc
pH 8.5, 30°C, continuous spectrophotometric assay
7
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
pH 8.5, 30°C, continuous spectrophotometric assay
7
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc
-
pH 8.5, 30°C
7
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc
-
pH 8.5, 30°C
5.4
GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc-beta-(1-4)-GlcNAc
-
pH 8.5, 30°C
1.53
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
pH 7.0, 37°C, fluorogenic labeling method assay
6
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
pH 8.5, 30°C, continuous spectrophotometric assay
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.2
recombinant His6-tagged enzyme in Pichia pastoris cell culture supernatant
135.6
purified recombinant His6-tagged enzyme, substrate penta-N-acetyl-chitopentaose
138.5
purified recombinant His6-tagged enzyme, substrate tetra-N-acetyl-chitotetraose
184.4
purified recombinant His6-tagged enzyme, substrate hexa-N-acetyl-chitohexaose
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
assay at, Pichia pastoris expressed recombinant enzyme, fluorogenic labeling method assay
8.5
assay at, Escherichia coli expressed recombinant enzyme, continuous spectrophotometric assay
8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
assay at, Escherichia coli expressed recombinant enzyme, continuous spectrophotometric assay
37
assay at, Pichia pastoris expressed recombinant enzyme, fluorogenic labeling method assay
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 75
half-maximal activity at 40°C and 75°C, 30% of maximal activity at 80°C
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
-
-
-
additional information
in fungi, periplasmic CDAs are generally tightly coupled to a chitin synthase to rapidly deacetylate newly synthesized chitins before their maturation and crystallization. Extracellular CDAs are secreted to alter the physicochemical properties of the cell wall to either protect the cell wall from exogenous chitinases or to initiate autolysis
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the carbohydrate esterases family 4 (CE4 enzymes) which includes chitin and peptidoglycan deacetylases, acetylxylan esterases, and poly-N-acetylglucosamine deacetylases that act on structural polysaccharides, altering their physicochemical properties, and participating in diverse biological functions. Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases, overview. Enzymatic action patterns for enzymes that modify in-chain units on a linear polysaccharide may be divided into three main types, designated multiple-attack, multiple-chain, and single-chain mechanisms
physiological function
chitin and peptidoglycan deacetylases are not only involved in cell wall morphogenesis and remodeling in fungi and bacteria, but they are also used by pathogenic microorganisms to evade host defense mechanisms. Likewise, biofilm formation in bacteria requires partial deacetylation of extracellular polysaccharides mediated by poly-N-acetylglucosamine deacetylases
additional information
the chitin deacetylase from Colletotrichum lindemuthianum follows the multiple-chain mechanism, in which the enzyme forms an active enzyme-polymer complex, and catalyzes the hydrolysis of only one acetyl group before it dissociates and forms a new active complex
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). CDA_COLLN
248
0
27041
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25200
x * 25200, recombinant His6-tagged enzyme, SDS-PAGE
150000
150000
-
amino acid and carbohydrate analysis in combination with data from SDS-PAGE and gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
S1-CDA: 24700, S1-CDAH: 25700, S12-CDAH: 26800, original CDA: 24300, SDS-PAGE
monomer
-
1 * 150000, amino acid and carbohydrate analysis in combination with data from SDS-PAGE and gel filtration
additional information
comparison of enzyme amino acid sequences of strain UPS9 with those of strain ATCC 56676, overview
additional information
-
comparison of enzyme amino acid sequences of strain UPS9 with those of strain ATCC 56676, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the enzyme contains a signal sequence which is cleaved at Gln28
glycoprotein
glycoprotein
-
galactose, mannose, xylose, fucose, N-acetyl-D-glucosamine, N-acetylgalactosamine, N-acetylneuraminic acid
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged enzyme expressed in Pichia pastoris, sitting drop vapour diffusion method, 20 mg/ml protein in 30 mM Tris-HCl, pH 8.0, is mixed with an equal volume of reservoir solution containing 30% w/v PEG 4000, 0.2 M ammonium acetate, and 0.1 M sodium acetate, pH 4.6, 20°C, 10 days, plate-like crystals, soaking of crystals in mother liquor with 10 mM ZnCl2, for 3 h, cryoprotection by 15% glycerol, flash freezing, and X-ray diffraction structure determination and analysis at 1.8 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme 364fold from Pichia pastoris strain GS115 culture supernatant by the single step process of nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His6-tagged enzyme in Pichia pastoris strain GS115, secretion of the recombinant enzyme to the culture supernatant
expression of the C-terminally His6-tagged enzyme in Pichia pastoris and in Escherichia coli, the His-tag causes intramolecular interactions with the active site
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
commercial wheat bran medium (pH 6.4) supplemented with chitosan favors maximal chitin deacetylase yield
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the enzyme might be useful for large scale production of chitosan from chitin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kauss, H.; Jeblick, W.; Young, D.H.
Chitin deacetylase from the plant pathogen Colletotrichum lindemuthianum
Plant Sci. Lett.
28
231-236
1983
Colletotrichum lindemuthianum, Rhizomucor miehei
-
Tokuyasu, K.; Ono, H.; Hayashi, K.; Mori, Y.
Reverse hydrolysis reaction of chitin deacetylase and enzymatic synthesis of beta-D-GlcNAc-(1-4)-GlcN from chitobiose
Carbohydr. Res.
322
26-31
1999
Colletotrichum lindemuthianum
Tokuyasu, K.; Ono, H.; Mitsutomi, M.; Hayashi, K.; Mori, Y.
Synthesis of a chitosan tetramer derivative, beta-D-GlcNAc-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc-(1-4)-D-GlcN through a partial N-acetylation reaction by chitin deacetylase
Carbohydr. Res.
325
211-215
2000
Colletotrichum lindemuthianum
Tokuyasu, K.; Kaneko, S.; Hayashi, K.; Mori, Y.
Production of a recombinant chitin deacetylase in the culture medium of Escherichia coli cells
FEBS Lett.
458
23-26
1999
Colletotrichum lindemuthianum
Tokuyasu, K.; Mitsutomi, M.; Yamaguchi, I.; Hayashi, K.; Mori, Y.
Recognition of chitooligosaccharides and their N-acetyl groups by putative subsites of chitin deacetylase from a deuteromycete, Colletotrichum lindemuthianum
Biochemistry
39
8837-8843
2000
Colletotrichum lindemuthianum
Tsigos, I.; Bouriotis, V.
Purification and characterization of chitin deacetylase from Colletotrichum lindemuthianum
J. Biol. Chem.
270
26286-26291
1995
Colletotrichum lindemuthianum
Tokuyasu, K.; Ohnishi-Kameyama, M.; Hayashi, K.
Purification and characterization of extracellular chitin deacetylase from Colletotrichum lindemuthianum
Biosci. Biotechnol. Biochem.
60
1598-1603
1996
Colletotrichum lindemuthianum
Hekmat, O.; Tokuyasu, K.; Withers, S.G.
Subsite structure of the endo-type chitin deacetylase from a deuteromycete, Colletotrichum lindemuthianum: an investigation using steady-state kinetic analysis and MS
Biochem. J.
374
369-380
2003
Colletotrichum lindemuthianum
Blair, D.E.; Hekmat, O.; Schuettelkopf, A.W.; Shrestha, B.; Tokuyasu, K.; Withers, S.G.; van Aalten, D.M.
Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum
Biochemistry
45
9416-9426
2006
Colletotrichum lindemuthianum (Q6DWK3), Colletotrichum lindemuthianum, Colletotrichum lindemuthianum UPS9 (Q6DWK3)
Shrestha, B.; Blondeau, K.; Stevens, W.F.; Hegarat, F.L.
Expression of chitin deacetylase from Colletotrichum lindemuthianum in Pichia pastoris: purification and characterization
Protein Expr. Purif.
38
196-204
2004
Colletotrichum lindemuthianum (Q6DWK3), Colletotrichum lindemuthianum, Colletotrichum lindemuthianum UPS9 (Q6DWK3), Colletotrichum lindemuthianum UPS9
Zhao, Y.; Park, R.D.; Muzzarelli, R.A.
Chitin deacetylases: properties and applications
Mar. Drugs
8
24-46
2010
Absidia caerulea, Amylomyces rouxii, Anopheles gambiae, Apis mellifera, Aspergillus nidulans, Colletotrichum lindemuthianum, Cryptococcus neoformans, Drosophila melanogaster, Flammulina velutipes, Helicoverpa armigera, Mamestra configurata, Metarhizium anisopliae, Mortierella sp., Rhizopus circinans, Rhizopus stolonifer, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Scopulariopsis brevicaulis, Tribolium castaneum, Trichoplusia ni, Vibrio cholerae serotype O1
Suresh, P.; Sachindra, N.; Bhaskar, N.
Solid state fermentation production of chitin deacetylase by Colletotrichum lindemuthianum ATCC 56676 using different substrates
J. Food Sci. Technol.
48
349-356
2011
Colletotrichum lindemuthianum, Colletotrichum lindemuthianum ATCC 56676
Kang, L.; Liang, Y.; Ma, L.
Novel characteristics of chitin deacetylase from Colletotrichum lindemuthianum: production of fully acetylated chitooligomers, and hydrolysis of deacetylated chitooligomers
Process Biochem.
49
1936-1940
2014
Colletotrichum lindemuthianum
-
Aragunde, H.; Biarnes, X.; Planas, A.
Substrate recognition and specificity of chitin deacetylases and related family 4 carbohydrate esterases
Int. J. Mol. Sci.
19
E412
2018
Amylomyces rouxii (P50325), Arthrobacter sp. Hiyo8 (A0A0K2RH66), Aspergillus nidulans (B3VD85), Colletotrichum lindemuthianum (Q6DWK3), Pestalotiopsis sp. (A0A1L3THR9), Pochonia chlamydosporia (A0A179EY19), Pochonia chlamydosporia 170 (A0A179EY19), Podospora anserina, Puccinia graminis f. sp. tritici (H6QRV0), Puccinia graminis f. sp. tritici CRL 75-36-700-3 (H6QRV0), Puccinia graminis f. sp. tritici race SCCL (H6QRV0), Sinorhizobium meliloti (P02963), Vibrio cholerae, Vibrio parahaemolyticus
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