Any feedback?
Information on EC 3.2.1.132 - chitosanase and Organism(s) Streptomyces sp. and UniProt Accession P33665
for references in articles please use BRENDA:EC3.2.1.132Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.132 chitosanaseIUBMB Comments
A whole spectrum of chitosanases are now known (for more details, see {http://rbrzezinski.recherche.usherbrooke.ca/::http://rbrzezinski.recherche.usherbrooke.ca/}). They can hydrolyse various types of links in chitosan. The only constant property is the endohydrolysis of GlcN-GlcN links, which is common to all known chitosanases. One known chitosanase is limited to this link recognition , while the majority can also recognize GlcN-GlcNAc links or GlcNAc-GlcN links but not both. They also do not recognize GlcNAc-GlcNAc links in partly acetylated chitosan.
Specify your search results
Word Map
- 3.2.1.132
- chitosans
- chitooligosaccharides
-
deacetylation
- oligosaccharide
- glycoside
-
colloidal
- chitinases
-
glcn
-
endo-type
-
biocontrol
- paenibacillus
- circulans
- chitotetraose
-
chitosanolytic
- d-glucosamine
- food industry
-
chitinolytic
- chitotriose
- synthesis
- biotechnology
- glucanase
- analysis
- industry
- pharmacology
- coss
- medicine
- chitopentaose
-
chitooligomers
- lichenan
- microbacterium
- agriculture
The taxonomic range for the selected organisms is: Streptomyces sp.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
=
+
+
=
+
Synonyms
chitosanase, csnts, endo-chitosanase, chitosanase ii, gscsn46a, family 46 chitosanase, chit b, csnw2, endochitosanase, chit a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
chitosan N-acetylglucosaminohydrolase
A whole spectrum of chitosanases are now known (for more details, see {http://rbrzezinski.recherche.usherbrooke.ca/::http://rbrzezinski.recherche.usherbrooke.ca/}). They can hydrolyse various types of links in chitosan. The only constant property is the endohydrolysis of GlcN-GlcN links, which is common to all known chitosanases. One known chitosanase is limited to this link recognition [4], while the majority can also recognize GlcN-GlcNAc links or GlcNAc-GlcN links but not both. They also do not recognize GlcNAc-GlcNAc links in partly acetylated chitosan.
CAS REGISTRY NUMBER
COMMENTARY
51570-20-8
-
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-methylumbelliferyl beta-chitotrioside + H2O
4-methylumbelliferone + chitotriose + chitobiose + 4-methylumbelliferyl N-acetyl-beta-D-glucosaminide
-
-
-
-
?
chitohexaose + H2O
chitobiose + chitotriose + chitotetraose
-
-
mutant enzyme D57A produces smaller amounts of chitobiose and chitotetraose as compared to chitotriose than does the wild-type enzyme
-
?
chitosan + H2O
?
-
chitosan of approximately 100 kDa and degree of deacetylation 96%
-
-
?
chitosan + H2O
?
the wild type chitosanase shows a clear preference for chitosan with high degrees of N-deacetylation (84-97%)
-
-
?
chitosan + H2O
chitosan oligosaccharides
-
-
products are a variety of oligomers
-
?
chitosan + H2O
chitosan oligosaccharides
-
substrate with average molecular weight of 220 kDA, 85% deacetylated
-
-
?
chitosan pentasaccharide + H2O
?
-
92% deacetylated chitosan, development of a Remazol Brilliant Blue R dye-coupled, quantitative enzyme assay method, overview
-
-
?
chitosan + H2O
additional information
-
-
-
diglucosamine and triglucosamine
?
chitosan + H2O
additional information
-
-
the smallest of the substrates is a tetramer of glucosamine
mixture of dimer and trimer of glucosamine
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
additional information
?
-
-
chitosan crosslinked with trimellitic anhydride, diisocyanatohexane, and dibromodecane show the same hydrolytic behaviour as uncrosslinked chitosan. Crosslinked chitosan species which are complexed with metals exhibits a significantly reduced extent of hydrolysis
-
-
?
additional information
?
-
the enzyme does not react with chitin. Oligosaccharides with degree of polymerization above 4 are not hydrolyzed
-
-
?
additional information
?
-
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis. The preferred cleavage site of enzyme CSN2 is between GlcN(Ac) and GlcN(Ac)
-
-
?
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
chitosan + H2O
?
the wild type chitosanase shows a clear preference for chitosan with high degrees of N-deacetylation (84-97%)
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
0.688 mg/ml chitosan, at pH 5.5
-
additional information
additional information
-
0.688 mg/ml chitosan, at pH 5.5
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.9
chitosan
mutant enzyme R42K, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
1.6
chitosan
mutant enzyme R42E at 37°C in 50 mM sodium acetate buffer (pH 5.5)
10
chitosan
chitosan with less than 75% deacetylation, at pH 6.0 and 45°C
10.7
chitosan
wild type enzyme, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
11.2
chitosan
chitosan with more than 90% deacetylation, at pH 6.0 and 45°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0012
mutant enzyme D40G/R42E, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
0.018
mutant enzyme D40G/R42K, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
0.9
mutant enzyme R42E at 37°C in 50 mM sodium acetate buffer (pH 5.5)
1.4
mutant enzyme R42K, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
1.6
mutant enzyme D40G, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
105
52.9
wild type enzyme, at 37°C in 50 mM sodium acetate buffer (pH 5.5)
59.8
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6
5.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
above, complete loss of activity due to partial denaturation of enzyme and chitosan substrate insolubilization
additional information
-
study on the interaction of pH value with activity. Reaction rate decreases by 50% from pH 5.5 to 6.0
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop crystallization with 30 mg/ml protein in 20 mM acetate, pH 5.5 mixed with 0.1 volume of a 0.5 M potassium phosphate, 20% w/v PEG 8000 solution, monoclinic space group P21
-
sitting drop vapor diffusion method, using 10% (w/v) MEPEG 5K, 300 mM tetramethylammonium chloride, and 100 mM Bis-Tris, pH 6.5, at 4°C
the substrate binding cleft is composed of six monosaccharide binding subsites
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D40G
D57A
D57N
W101F
W227F
W28F
additional information
-
consensus enzyme mutant designed by multiple amino acid substitutions. Increase in transition temperature
D57A
-
mutant enzyme shows 0.5% of wild-type activity. Mutant enzyme D57A produces smaller amounts of chitobiose and chitotetraose as compared to chitotriose than does the wild-type enzyme
W101F
-
no effect to the activity in hydrolysing chitohexaose, but just 70-90% activity against 30% acetylated chitosan in contrast to the wild-type enzyme
W227F
-
no effect to the activity in hydrolysing chitohexaose, but just 70-90% activity against 30% acetylated chitosan in contrast to the wild-type enzyme
W28F
-
no effect to the activity in hydrolysing chitohexaose, but just 70-90% activity against 30% acetylated chitosan in contrast to the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
81.1
-
consensus mutant, transition temperature in presence of chitosan at 6 g/l
83.3
-
mutant A104L, transition temperature in presence of chitosan at 6 g/l
85.1
-
mutant K164R, transition temperature in presence of chitosan at 6 g/l
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Streptomyces lividans strain TK24 by ion exchange and hydroxylapatite chromatography
-
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Streptomyces lividans strain TK24 and Escherichia coli Gold cells
expression in Streptomyces lividans TK24
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
fluorimetric determination of transition temperature is a reliable method for rapid assessment of the thermal behaviour of chitosanases and applicable to structure-function studies
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Price, J.S.; Storck, R.
Production, purification, and characterization of an extracellular chitosanase from Streptomyces
J. Bacteriol.
124
1574-1585
1975
Streptomyces sp., Streptomyces sp. No. 6
Boucher, I.; Dupuy, A.; Vidal, P.; Neugebauer, W.A.; Brzezinski, R.
Purification and characterization of a chitosanase from Streptomyces N174
Appl. Microbiol. Biotechnol.
38
188-193
1992
Streptomyces sp.
-
Marcotte, E.; Hart, P.J.; Boucher, I.; Brzezinski, R.; Robertus, J.D.
Crystallization of a chitosanase from Streptomyces N174
J. Mol. Biol.
232
995-996
1993
Streptomyces sp.
Tremblay, H.; Yamaguchi, T.; Fukamizo, T.; Brzezinski, R.
Mechanism of chitosanase-oligosaccharide interaction: subsite structure of Streptomyces sp. N174 chitosanase and the role of Asp57 carboxylate
J. Biochem.
130
679-686
2001
Streptomyces sp.
Fukamizo, T.; Brzezinski, R.
Chitosanase from Streptomyces sp. strain N174: a comparative review of its structure and function
Biochem. Cell Biol.
75
687-696
1997
Streptomyces sp.
Fukamizo, T.; Honda, Y.; Goto, S.; Boucher, I.; Brzezinski, R.
Reaction mechanism of chitosanase from Streptomyces sp. N174
Biochem. J.
311
377-383
1995
Streptomyces sp.
Honda, Y.; Fukamizo, T.; Okajima, T.; Goto, S.; Boucher, I.; Brzezinski, R.
Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization
Biochim. Biophys. Acta
1429
365-376
1999
Streptomyces sp. (P33665)
Honda, Y.; Kirihata, M.; Fukamizo, T.; Kaneko, S.; Tokuyasu, K.; Brzezinski, R.
Chitosanase-catalyzed hydrolysis of 4-methylumbelliferyl beta-chitotrioside
J. Biochem.
126
470-474
1999
Streptomyces sp.
Marcotte, E.M.; Monzingo, A.F.; Ernst, S.R.; Brzezinski, R.; Robertus, J.D.
X-ray structure of an anti-fungal chitosanase from streptomyces N174
Nat. Struct. Biol.
3
155-162
1996
Streptomyces sp.
Fukamizo, T.; Yamaguchi, T.; Tremblay, H.; Brzezinski, R.
Substrate binding mechanism of chitosanase from Streptomyces sp. N174
Adv. Chitin Sci.
4
575-581
2000
Streptomyces sp.
-
Somashekar, D.; Joseph, R.
Chitosanases-properties and applications: a review
Biores. Technol.
55
35-45
1996
Amycolatopsis orientalis, Amycolatopsis sp., Amylomyces rouxii, Bacillus licheniformis, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) K-1, Bacillus sp. (in: Bacteria) No. 7-M, Bacillus sp. (in: Bacteria) PI-7S, Bacillus sp. (in: Bacteria) R-4, Enterobacter sp., Fusarium solani, Myxobacter sp. AL-1, Niallia circulans, Niallia circulans MH-K1, Priestia megaterium, Pseudomonas sp., Pseudomonas sp. H-14, Rhodotorula toruloides, Streptomyces griseus, Streptomyces sp., Streptomyces sp. No. 6, Talaromyces islandicus
-
Katsumi, T.; Lacombe-Harvey, M.E.; Tremblay, H.; Brzezinski, R.; Fukamizo, T.
Role of acidic amino acid residues in chitooligosaccharide-binding to Streptomyces sp. N174 chitosanase
Biochem. Biophys. Res. Commun.
338
1839-1844
2005
Streptomyces sp.
Fukamizo, T.; Yoshikawa, T.; Katsumi, T.; Amano, S.; Saito, J.; Miki, K.; Ando, A.; Brzezinski, R.
Substrate-binding mode of bacterial chitosanases
J. Appl. Glycosci.
52
183-189
2005
Niallia circulans, Streptomyces sp., Niallia circulans MH-K1
-
Roy, S.; Fortin, M.; Gagnon, J.; Ghinet, M.G.; LeHoux, J.; Dupuis, G.; Brzezinski, R.
Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases
Biochim. Biophys. Acta
1774
975-984
2007
Streptomyces sp., Streptomyces coelicolor
Trimukhe, K.D.; Bachate, S.; Gokhale, D.V.; Varma, A.J.
Metal complexes of crosslinked chitosans Part II. An investigation of their hydrolysis to chitooligosaccharides using chitosanase
Int. J. Biol. Macromol.
41
491-496
2007
Streptomyces sp.
Lin Teng Shee, F.; Arul, J.; Brunet, S.; Bazinet, L.
Effect of bipolar membrane electrobasification on chitosanase activity during chitosan hydrolysis
J. Biotechnol.
134
305-311
2008
Streptomyces sp., Streptomyces sp. 174
Zitouni, M.; Fortin, M.; Thibeault, J.; Brzezinski, R.
A dye-labelled soluble substrate for the assay of endo-chitosanase activity
Carbohydr. Polym.
80
522-525
2010
Streptomyces sp.
-
Lacombe-Harvey, M.E.; Fortin, M.; Ohnuma, T.; Fukamizo, T.; Letzel, T.; Brzezinski, R.
A highly conserved arginine residue of the chitosanase from Streptomyces sp. N174 is involved both in catalysis and substrate binding
BMC Biochem.
14
23
2013
Streptomyces sp. (P33665)
Takasuka, T.E.; Bianchetti, C.M.; Tobimatsu, Y.; Bergeman, L.F.; Ralph, J.; Fox, B.G.
Structure-guided analysis of catalytic specificity of the abundantly secreted chitosanase SACTE_5457 from Streptomyces sp. SirexAA-E
Proteins
82
1245-1257
2014
Streptomyces sp. (G2NRC4), Streptomyces sp. SirexAA-E (G2NRC4)
EXTERNAL LINKS (specific for EC-Number 3.2.1.132)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
