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Information on EC 3.2.1.132 - chitosanase and Organism(s) Pseudomonas sp. A-01 and UniProt Accession Q8KZM5
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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: Pseudomonas sp. A-01
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
=
+
+
=
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Synonyms
chitosanase, endo-chitosanase, csnts, chitosanase ii, gscsn46a, family 46 chitosanase, csnw2, endochitosanase, chit a, chit b, 
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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
?
substrate recognition mechanismis for non-processive chitosanase is decribed
-
-
?
glycol chitosan + H2O
?
activity is ca. 4fold higher than toward chitosan
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-
?
N-acetylated chitosan + H2O
?
activity is ca. 3fold less than toward chitosan
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
1 mM completely inhibits, with colloidal chitosan as substrate
Hg2+
1 mM completely inhibits, with colloidal chitosan as substrate
additional information
1 mM Mg2+, Ca2+, Fe3+, Zn2+, Ba2+ and Pb2+ have little or no effect on activity
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D235A
with chitohexaose the mutant enzyme shows about 10% enhanced activity as compared to wild-type enzyme
D25A
with chitohexaose as substrate the mutant enzyme shows about 10% of the activity as compared to wild-type enzyme
D40A
with polymeric substrate the mutant enzyme shows less than 10% of the activity as compared to wild-type enzyme. With chitohexaose as substrate the mutant enzyme shows about 70% of the activity as compared to wild-type enzyme
D41N
hydrolyzing activity against 100% deacetylated chitin is severely affected
D43A
with chitohexaose as substrate the mutant enzyme shows about 10% of the activity as compared to wild-type enzyme
D60E
with chitohexaose as substrate the mutant enzyme shows about 5% of the activity as compared to wild-type enzyme
D91A
with polymeric substrate the mutant enzyme shows about 10% enhanced activity as compared to wild-type enzyme. With chitohexaose as substrate the mutant enzyme shows about 70% of the activity as compared to wild-type enzyme
E120A
with polymeric substrate the mutant enzyme shows about 40% enhanced activity as compared to wild-type enzyme. With chitohexaose the mutant enzyme shows about 40% enhanced activity as compared to wild-type enzyme
E23Q
hydrolyzing activity against 100% deacetylated chitin is severely affected
E39A
with polymeric substrate the mutant enzyme shows about 50% enhanced activity as compared to wild-type enzyme
E63A
with polymeric substrate the mutant enzyme shows about 35% enhanced activity as compared to wild-type enzyme. With chitohexaose the mutant enzyme shows about 20% enhanced activity as compared to wild-type enzyme
H203A
with chitohexaose as substrate the mutant enzyme shows no activity
T58A
with chitohexaose as substrate the mutant enzyme shows about 90% of the activity as compared to wild-type enzyme
Y233A
with polymeric substrate the mutant enzyme shows less than 10% of the activity as compared to wild-type enzyme. With chitohexaose the mutant enzyme shows about 10% enhanced activity as compared to wild-type enzyme
Y37F
with chitohexaose as substrate the mutant enzyme shows about 95 % of the activity as compared to wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by two consecutive anion exchange chromatography steps and subsequent reverse-phase column chromatography, to homogeneity, 65fold with a yield of 1.7%
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutants overexpressed in Brevibacillus choshinensis HDP31-M3 carrying the cto1 gene on expression plasmid vector pNCMO2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ando, A.; Saito, A.; Arai, S.; Usuda, S.; Furuno, M.; Kaneko, N.; Shida, O.; Nagata, Y.
Molecular characterization of a novel family-46 chitosanase from Pseudomonas sp. A-01
Biosci. Biotechnol. Biochem.
72
2074-2081
2008
Pseudomonas sp. A-01 (Q8KZM5)
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