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Information on EC 3.2.1.132 - chitosanase and Organism(s) Niallia circulans and UniProt Accession P33673
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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.
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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: Niallia circulans
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, endo-chitosanase, csnts, chitosanase ii, gscsn46a, family 46 chitosanase, endochitosanase, chit a, chit b, csnw2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
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
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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
chitosan + H2O
?
a chitosanase classification system is suggested which is based on specificities and preferences of subsites (-2) to (+2)
-
-
?
chitosan + H2O
GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcN + GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN
chitosan with 85% degree of deacetylation. Inserting two surface loops, the endo-type chitosanase Csn is converted into an exo-type chitosanase. The chimeric chitosanase has 3% of wild-type activity and GlcNbeta(1-4)GlcN is the dominant product, whereas a mixture of GlcNbeta(1-4)GlcN, GlcNbeta(1-4)GlcNbeta(1-4)GlcN and GlcNbeta(1-4)GlcNbeta(1-4)GlcNbeta(1-4)GlcN is obtained with the wild-type endo-chitosanase. Chimeric Csn catalyzes the hydrolysis of chitosan with a smaller rate of viscosity decrease than the wild-type
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-
?
chitosan + H2O
additional information
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-
the smallest of the substrates is a tetramer of glucosamine
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
substrates with less than 40% deacetylation are not affected by the enzyme
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
most susceptible substrate is: 80% deacetylated chitosan
mixture of dimer and trimer of glucosamine
?
chitosan + H2O
additional information
-
-
hydrolysis of: glycol chitosan
mixture of dimer and trimer of glucosamine
?
additional information
?
-
-
no activity with chitin (i.e. 100% acetylated chitosan)
-
-
?
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.2
9.2
-
density gradient column electrofocusing and acrylamide gel electrofocusing
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
citosanase inhibits the growth of zygomycetes fungi Rhizopus and Mucor probably via its fungistatic effect
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method at 20°C, orthorhombic space group P21212, two globular upper and lower domains which generate the active site cleft for the substrate binding
sitting drop vapor diffusion method at 20°C. The crystal structure of mutant K218P reveals that the main chain and side chain structures of the loop comprising Lys218 are effected by the mutation. It is concluded that the flexible loop comprising Lys128 plays an important role in substrate binding
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K218P
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mutant enzyme shows 0.16% of wild-type activity with acetylated chitosan
Y148S
-
mutant enzyme shows 12% of wild-type activity with acetylated chitosan
additional information
chimeric chitosanase produced by inserting two peptide loops, each containing a cysteine residue, in opposite walls of the substrate-binding cleft. The two cysteine residues form a disulfide bond crossing the protruding loop, which may alter the binding topology of the substrate and consequently convert the endo-chitosanase into an exo-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimeric chitosanase and wild-type Csn purified nearly to homogeneity by cation-exchange chromatography
CM-Toyopearl 650 M column chromatography and Resource S column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimeric chitosanase and wild-type Csn overexpressed from vector pET22b(+) in Escherichia coli strain BL21 (DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
chitosanases can be used to produce partially acetylated chitosan oligosaccharides for different applications
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yabuki, M.; Uchiyama, A.; Suzuki, K.; Ando, A.; Fujii, T.
Purification and properties of chitosanase from Bacillus circulans MH-K1
J. Gen. Appl. Microbiol.
34
255-270
1988
Niallia circulans, Niallia circulans MH-K1
-
Ando, A.; Noguchi, K.; Yanagi, M.; Shinoyama, H.; Kagawa, Y.; Hirata, H.; Yabuchi, M.; Fujii, T.
Primary structure of chitosanase produced by Bacillus circulans MH-K1
J. Gen. Appl. Microbiol.
38
135-144
1992
Niallia circulans, Niallia circulans MH-K1
-
Saito, J.; Kita, A.; Higuchi, Y.; Nagata, Y.; Ando, A.; Miki, K.
Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism
J. Biol. Chem.
274
30818-30825
1999
Niallia circulans (P33673), Niallia circulans MH-K1 (P33673)
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
-
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
-
Fukamizo, T.; Amano, S.; Yamaguchi, K.; Yoshikawa, T.; Katsumi, T.; Saito, J.; Suzuki, M.; Miki, K.; Nagata, Y.; Ando, A.
Bacillus circulans MH-K1 chitosanase: amino acid residues responsible for substrate binding
J. Biochem.
138
563-569
2005
Niallia circulans (P33673), Niallia circulans MH-K1 (P33673)
Yao, Y.Y.; Shrestha, K.L.; Wu, Y.J.; Tasi, H.J.; Chen, C.C.; Yang, J.M.; Ando, A.; Cheng, C.Y.; Li, Y.K.
Structural simulation and protein engineering to convert an endo-chitosanase to an exo-chitosanase
Protein Eng. Des. Sel.
21
561-566
2008
Niallia circulans (P33673), Niallia circulans MH-K1 (P33673)
Tomita, M.; Kikuchi, A.; Kobayashi, M.; Yamaguchi, M.; Ifuku, S.; Yamashoji, S.; Ando, A.; Saito, A.
Characterization of antifungal activity of the GH-46 subclass III chitosanase from Bacillus circulans MH-K1
Antonie van Leeuwenhoek
104
737-748
2013
Niallia circulans, Niallia circulans MH-K1
Weikert, T.; Niehues, A.; Cord-Landwehr, S.; Hellmann, M.J.; Moerschbacher, B.M.
Reassessment of chitosanase substrate specificities and classification
Nat. Commun.
8
1698
2017
Bacillus sp. No.7-M, Streptomyces sp. N174 (P33665), Niallia circulans (P33673), Niallia circulans MH-K1 (P33673)
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