3.2.1.132: chitosanase
This is an abbreviated version!
For detailed information about chitosanase, go to the full flat file.
Word Map on EC 3.2.1.132
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3.2.1.132
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chitosans
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chitooligosaccharides
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deacetylation
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oligosaccharide
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glycoside
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colloidal
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chitinases
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glcn
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endo-type
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biocontrol
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paenibacillus
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circulans
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chitotetraose
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chitosanolytic
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d-glucosamine
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food industry
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chitinolytic
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chitotriose
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synthesis
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biotechnology
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glucanase
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analysis
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industry
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pharmacology
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coss
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medicine
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chitopentaose
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chitooligomers
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lichenan
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microbacterium
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agriculture
- 3.2.1.132
- chitosans
- chitooligosaccharides
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deacetylation
- oligosaccharide
- glycoside
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colloidal
- chitinases
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glcn
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endo-type
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biocontrol
- paenibacillus
- circulans
- chitotetraose
-
chitosanolytic
- d-glucosamine
- food industry
-
chitinolytic
- chitotriose
- synthesis
- biotechnology
- glucanase
- analysis
- industry
- pharmacology
- coss
- medicine
- chitopentaose
-
chitooligomers
- lichenan
- microbacterium
- agriculture
Reaction
Synonyms
actase, AsChi, BspCsnMN, Cel7A, Cel8A, ChA, CHI, ChiN, Chit A, Chit B, chitosan N-acetylglucosaminohydrolase, chitosanase, chitosanase 1, chitosanase CsnA, chitosanase EAG1, chitosanase II, chitosanase OU01, ChiX, CHO, Cho-GG, ChoK, Chs1, Csn, CSN-174, CSN-7M, Csn-PD, Csn1, Csn2, CsnA, CsnB, CsnM, CSNMHKI, CsnN174, CsnTS, csnw2, Cto1, CtoA, Culf-Z, endo-acting chitinase, endo-chitosanase, endochitosanase, family 46 chitosanase, GH-75 chitosanase, GsCsn46A, ImmB-Z, MH-K1 chitosanase, More, mschito, N174 chitosanase, PgChP, SACTE_5457, SCO0677, StrCSN1, StrCSN2, TKU032 chitosanase
ECTree
3.2.1.132 chitosanaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.132 - chitosanase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E22Q
abolished chitosanase activity, does not exhibit antifungal activity
I13T/A87V
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DNA shuffling of the genes from strains KNUC51 and KNUC55, the shuffled product YM18 shows higher activity than the parents at 40°C. The specific activity of YM18 is enhanced 250% compared to the parents
K66R/N352S
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DNA shuffling of the genes from strains KNUC51 and KNUC55, the shuffled product YM20 shows higher activity than the parents at 40°C. The specific activity of YM20 is enhanced 350% compared to the parents, YM20 exhibits a shift of the optimal pH level from pH 5.5 to pH 6.5
E309R/N319E
the mutant enzyme can accept N-acetyl-D-glucosamine units at their subsite (-2), which is impossible for the wild-type enzyme
N308V/E309R/N319E
the mutant enzyme can accept N-acetyl-D-glucosamine units at their subsite (-2), which is impossible for the wild-type enzyme
D318N
mutant enzyme shows enhanced specific activity relative to wild-type chitosanase
D175E
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48.3% of wild-type activity with acetylated chitosan as substrate (acetylation degree: 30%)
D212N
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37.9% of wild-type activity with acetylated chitosan as substrate (acetylation degree: 30%)
E188D
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23.6% of wild-type activity with acetylated chitosan as substrate (acetylation degree: 30%)
G151D
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inactive. Use of strain for isolation of mutant genes with restored activity
G151D/N222S
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mutant with restored activity based on inactive mutant G151D, 1.2 fold higher in specific activity than wild-type and 17% increase in thermal stability at 50°C
L74Q/V75I/G151D
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mutant with restored activity based on inactive mutant G151D, 1.5fold higher in specfic activity than wild-type, and protein is efficiently secreted
G151D
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inactive. Use of strain for isolation of mutant genes with restored activity
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G151D/N222S
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mutant with restored activity based on inactive mutant G151D, 1.2 fold higher in specific activity than wild-type and 17% increase in thermal stability at 50°C
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L74Q/V75I/G151D
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mutant with restored activity based on inactive mutant G151D, 1.5fold higher in specfic activity than wild-type, and protein is efficiently secreted
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K218P
Y148S
K218P
Y148S
A207C/L286C
mutant enzyme has a longer half-life at 50°C (from 10.5 to 69.3 min) and a 200% higher catalytic efficiency (Kcat/Km) than that of the wild-type enzyme
G113C/D116C
at 50°C the wild-type shows less than 37% of the initial activity after 30 min, mutant enzyme G113C/D116C retains 62.0% of its initial activity
E302A
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302C
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302D
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302F
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302G
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302H
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302I
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302K
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302K/N312A
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302K/N312D
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302K/N312K
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site-directed mutagenesis, the mutant enzyme shows no beta-1,4 glucanase activity
E302K/N312R
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site-directed mutagenesis, the mutant enzyme shows no beta-1,4 glucanase activity
E302L
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302M
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302N
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302P
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302Q
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302R
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302R/N312A
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site-directed mutagenesis, the mutant enzyme shows no beta-1,4 glucanase activity
E302R/N312D
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302R/N312K
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site-directed mutagenesis, the mutant enzyme shows no beta-1,4 glucanase activity
E302R/N312R
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site-directed mutagenesis, the mutant enzyme shows no beta-1,4 glucanase activity
E302S
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302T
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302V
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
E302Y
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312A
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312D
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312K
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
N312R
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
W228A/Y311A
the mutant shows about 30% of wild type activity
E302A
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
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E302C
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
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E302K
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
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N312A
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site-directed mutagenesis, the mutant enzyme shows reduced beta-1,4 glucanase activity compared to the wild-type enzyme
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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
E160A
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mutant enzyme with decreased thermal stability and reduced specific activity
E160Q
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mutant enzyme with decreased thermal stability and reduced specific activity
K163A
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mutant enzyme with decreased thermal stability and reduced specific activity
T114A
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mutant enzyme with decreased thermal stability and slightly reduced specific activity
D40G
D57A
D57N
W101F
W227F
W28F
D201A
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time-course is almost identical to that obtained by the wild-type
D40G
D40G/T45D
reaction time is 100 min. It has 0.1% of wild-type specific activity when tested on chitosan substrate
D40G/T45E
has 0.03% of wild-type specific activity when tested on chitosan substrate
E36A/D40G
reaction time is 100 min. Kcat is ca. 18times lower than that of the single mutant D40G. Rate of (GlcN)6 degradation is enhanced by sodium azide
E36Q/D40G
reaction time is 100 min. Kcat is more than 5times lower than that of the single mutant D40G
T45E
has a very low residual activity. Activity of this mutant can not be enhanced by sodium azide
T45S
reaction time is 20 min. It is quite active, keeps ca. 71% of the specific activity of the wild-type enzyme
V148T
has 10% of wild-type activity when tested on chitosan substrate
additional information
K218P
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mutant enzyme shows 0.16% of wild-type activity with acetylated chitosan
Y148S
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mutant enzyme shows 12% of wild-type activity with acetylated chitosan
K218P
Niallia circulans MH-K1
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mutant enzyme shows 0.16% of wild-type activity with acetylated chitosan
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Y148S
Niallia circulans MH-K1
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mutant enzyme shows 12% of wild-type activity with acetylated chitosan
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D57A
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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
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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
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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
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no effect to the activity in hydrolysing chitohexaose, but just 70-90% activity against 30% acetylated chitosan in contrast to the wild-type enzyme
D40G
reaction time is 20 min. It is distinguished from wild-type by a lower activity, without changing the mechanism of hydrolysis or the mode of interaction with substrate
additional information
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knock down of chitosanase expression in phytopathogenic fungus Fusarium solani affects its pathogenicity
additional information
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knock down of chitosanase expression in phytopathogenic fungus Fusarium solani affects its pathogenicity
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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
additional information
Niallia circulans MH-K1
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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
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additional information
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establishing of a recombinant expression of the enzyme at the cell surface of Saccharomyces cerevisiae strain MT8-1 cells, using a yeast cell surface-displaying system, to facilitate enzyme purification
additional information
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mutational analysis of discoidin domain function
additional information
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establishing of a recombinant expression of the enzyme at the cell surface of Saccharomyces cerevisiae strain MT8-1 cells, using a yeast cell surface-displaying system, to facilitate enzyme purification
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additional information
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the fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5) exhibits higher chitosan binding capacity and catalytic activity than wild-type enzyme. The fusion of BgCBM5 significantly improves the thermostability of citosanase CsnA
additional information
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immobilization of chitosanase onto liposome for construction of a biocatalyst, the immobilized enzyme on liposomes shows increased activity and stability to pH and temperature, overview
additional information
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consensus enzyme mutant designed by multiple amino acid substitutions. Increase in transition temperature
