3.2.1.39: glucan endo-1,3-beta-D-glucosidase
This is an abbreviated version!
For detailed information about glucan endo-1,3-beta-D-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.39
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3.2.1.39
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chitinase
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glucans
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barley
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beta-glucans
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pathogenesis-related
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polysaccharide
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cellulase
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beta-1,3-glucans
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xylanase
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trichoderma
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elicitors
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chitin
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phytophthora
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biocontrol
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callose
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lichenan
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solani
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mannoproteins
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rhizoctonia
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transglycosylation
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defense-related
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thaumatin-like
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zymolyase
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digesta
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mycoparasitism
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harzianum
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laminaribiose
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mixed-linkage
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circulans
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capsici
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hemicellulase
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fibrobacter
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gentiobiose
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curdlan
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digitata
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carbohydrases
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laminaria
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pectinase
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neurexins
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pharmacology
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medicine
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synthesis
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food industry
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biotechnology
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agriculture
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analysis
- 3.2.1.39
- chitinase
- glucans
- barley
- beta-glucans
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pathogenesis-related
- polysaccharide
- cellulase
- beta-1,3-glucans
- xylanase
- trichoderma
- elicitors
- chitin
- phytophthora
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biocontrol
- callose
- lichenan
- solani
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mannoproteins
- rhizoctonia
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transglycosylation
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defense-related
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thaumatin-like
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zymolyase
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digesta
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mycoparasitism
- harzianum
- laminaribiose
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mixed-linkage
- circulans
- capsici
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hemicellulase
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fibrobacter
- gentiobiose
- curdlan
- digitata
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carbohydrases
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laminaria
- pectinase
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neurexins
- pharmacology
- medicine
- synthesis
- food industry
- biotechnology
- agriculture
- analysis
Reaction
Synonyms
(1-3)-beta-D-glucan endohydrolase, (1-3)-beta-D-glucanase, (1-3)-beta-glucanase GI, (1->3)-beta-glucan endohydrolase, (1->3)-beta-glucan endohydrolase BGN13.1, (1->3)-beta-glucan endohydrolase GI, (1->3)-beta-glucan endohydrolase GII, (1->3)-beta-glucan endohydrolase GIII, (1->3)-beta-glucan endohydrolase GIV, (1->3)-beta-glucan endohydrolase GV, (1->3)-beta-glucan endohydrolase GVI, (1->3)-beta-glucanase, (1->3)-beta-glucanase A1, (1->3)-beta-glucanase BGN13.1, (1->3)-beta-glucanase isoenzyme GI, (1->3)-beta-glucanase isoenzyme GII, (1->3)-beta-glucanase isoenzyme GIII, (1->3)-beta-glucanase isoenzyme GIV, (1->3)-beta-glucanase isoenzyme GV, (1->3)-beta-glucanase isoenzyme GVI, (13)-beta-glucan 3-glucanohydrolase, (13)-beta-glucan endohydrolase, 1,3-beta-D-glucanase, 1,3-beta-glucan 3-glucanohydrolase, 1,3-beta-glucan hydrolase, 1,3-beta-glucanase, 1,3-beta-glucanase I, Acidic beta-1,3-glucanase, acidic endo-beta-1,3-glucanase, AkLam36, Anther-specific protein A6, Ban-Gluc, Basic beta-1,3-endoglucanase BGN13.1, Basic beta-1,3-glucanase, beta-(1-3)-glucanase, beta-1,3 glucanase, beta-1,3-D-glucanase, beta-1,3-endoglucanase, Beta-1,3-endoglucanase GI, Beta-1,3-endoglucanase GII, Beta-1,3-endoglucanase GIII, Beta-1,3-endoglucanase GIV, Beta-1,3-endoglucanase GV, Beta-1,3-endoglucanase GVI, Beta-1,3-endoglucanase, basic, beta-1,3-glucan hydrolase, beta-1,3-glucanase, beta-1,3-glucanase I, beta-1,3-glucanase II, beta-glucanase, Bgl, Bgl2, Bgl64A, BglF, BglII, BglS27, Bglu50A, Bgt17AE158A, CaENG, callase, CC1G_04051, CcGluE, Cel17A, DEHA2G18766g, DEHA2G18766p, EGase1, EGase2, EGase3, endo-(1,3)-beta-D-glucanase, endo-(1-3)-beta-glucanase, endo-(13)-beta-D-glucanase, endo-1,3-beta-D-glucanase, endo-1,3-beta-glucanase, endo-1,3-beta-glucosidase, endo-1,3-glucanase, endo-1,3;4-beta-glucanase, endo-beta-1,3(4)-glucanase, endo-beta-1,3-D-glucanase, endo-beta-1,3-glucanase, endo-beta-1->3-glucanase, endo-type beta-1,3-glucanase, Endo23, Eng, eng1, ENG16A, Eng2, Eng2 protein, EngA, Engl1, exo-beta-1,3-glucanase, Fra e 9.01 allergen, Gbl2a, Gbl2b, Gbl2c, Gbl2d, Gbl2e, Gbl2f, Gbl3, Gfa, GH family 81 beta-1,3-glucanase, GLU, Glu1, GluA, GLUB20-2, glucan endo-1,3-beta-glucosidase, Glucanase GLA, Glucanase GLB, glucanase LIV, glucanase Lo, GLUD2, HdLam33, kitalase, LAM, Lam81A, LamA, laminaranase, laminarinase, Lic16A, lytic beta-(1-3)-glucanase I, lytic beta-(1-3)-glucanase II, Mo enzyme, More, oligo-1,3-glucosidase, OsGlu1, OsGlu2, PCEng2p, PfLamA, PpGns1, PR-2B, PR-35, PR-36, PR-37, Rv0315, SLam, SpsLamIV, TLam, TmLam, VIT_05s0077g01150, VIT_205s0077g01150, VIT_206s0061g00120, VIT_208s0007g06060, YlCrh1Sp, YlCrh2Sp, zerzaust, ZET, ZgLamA
ECTree
3.2.1.39 glucan endo-1,3-beta-D-glucosidaseAdvanced search results
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results (Engineering
Engineering on EC 3.2.1.39 - glucan endo-1,3-beta-D-glucosidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
E119A
E119A/Ldel
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variant of catalytic domain with deletion of the Gly/Ser-rich linker, Ser244-Thr256, no expression of protein
E119G
site-directed mutagenesis, glucosidase inactive catalytic residue mutant, the mutant shows transglycosylation activity toward laminarioligosaccharides. The hydrolytic as well as transglycosylation activities of E119G decrease with the decrease in temperature, but the ratio of transglycosylation products increases. The enzymatic activity of E119G toward laminaritriose in the presence of glucose is abolished, while the addition of laminaribiose evidently increases the transglycosylation products such as laminaritetraose and laminaripentaose
M123del
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variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
E119A
E119A/Ldel
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variant of catalytic domain with deletion of the Gly/Ser-rich linker, Ser244-Thr256, no expression of protein
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E119G
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site-directed mutagenesis, glucosidase inactive catalytic residue mutant, the mutant shows transglycosylation activity toward laminarioligosaccharides. The hydrolytic as well as transglycosylation activities of E119G decrease with the decrease in temperature, but the ratio of transglycosylation products increases. The enzymatic activity of E119G toward laminaritriose in the presence of glucose is abolished, while the addition of laminaribiose evidently increases the transglycosylation products such as laminaritetraose and laminaripentaose
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M123del
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variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
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E231A
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no enzymic activity with laminarin, in presence of sodium formate, recovery of 75% of activitiy compared to wild type, with substrate alpha-laminaribiosyl fluoride, polymerization to insoluble, crystalline (1,3)-beta-D-glucans
E231G
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no enzymic activity with laminarin, in presence of sodium formate, recovery of 75% of activitiy compared to wild type, with substrate alpha-laminaribiosyl fluoride, polymerization to insoluble, crystalline (1,3)-beta-D-glucans
E231S
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no enzymic activity with laminarin, with substrate alpha-laminaribiosyl fluoride, polymerization to insoluble, crystalline (1,3)-beta-D-glucans
W118A
H245A
W1679A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1688A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1729A
site-directed mutagenesis, mutation in the F5/8C module or DS domain, the mutant domain forms inclusion bodies upon expression in Escherichia coli
Y1714A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
Y1768A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1679A
Paenibacillus sp. CCRC 17245 BCRC
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site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
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W1688A
Paenibacillus sp. CCRC 17245 BCRC
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site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
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W1729A
Paenibacillus sp. CCRC 17245 BCRC
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site-directed mutagenesis, mutation in the F5/8C module or DS domain, the mutant domain forms inclusion bodies upon expression in Escherichia coli
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Y1714A
Paenibacillus sp. CCRC 17245 BCRC
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site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
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Y1768A
Paenibacillus sp. CCRC 17245 BCRC
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site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
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delI72-G75
deletion mutant, lacking residues 72-75, hydrolyses the mixed-linkage beta-1,3-1,4-glucan lichenan at 40°C and 70°C 10times more efficiently than the wiild-type protein. At 80°C, the specific activity of the D-loop mutant is reduced significantly relative to that of the wild-type with both laminarin and lichenan
delMet174
the specific activities of the mutant LamA, on both laminarin and lichenan, is about 10fold lower than the respective wild-type value. The methionine deletion leads to an enzyme with 13.1% of wild-type Vmax and a slightly higher Km on laminarin as a substrate. With lichenan as substrate, the mutant LamA has 7.9% of the wild-type Vmax and the same Km value
E170A
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severely reduced hydrolytic activity, active as a glycosynthase catalysing condensation of alpha-laminaribiosyl fluoride to different acceptors
S296C
the immobilized S296C variant shows extreme pH stability and can be repeatedly used at 60°C without significant activity loss of activity
E158A
D526A
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enzymatic activity is similar to that of the wild type protein
D545A
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enzymatic activity is similar to that of the wild type protein
D526A
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enzymatic activity is similar to that of the wild type protein
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C6A
significant decrease in activity towards carboxymethyl-curdlan and laminarin, strong increase in activity towards lichenan
E259A
site-directed mutagenesis, substitution of the nucleophilic residue, the active site mutant retains residual endoglucanase activity
D422A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D422E
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D424A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D424H
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site-directed mutagenesis, the mutation alters the substrate specificity by increasing the rate of cleavage of mixed-linkage beta-glucan and carboxymethylcellulose 60fold and 16fold, respectively, compared to the wild-type enzyme
D424H/S501A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E499A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E499D
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E503A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E503D
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
F425A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
F425Y
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
H423A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
H426A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
N421A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
S500A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
S501A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
S502A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
W404A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
W444A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
Y427A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D422A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
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D424A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
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D424H
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site-directed mutagenesis, the mutation alters the substrate specificity by increasing the rate of cleavage of mixed-linkage beta-glucan and carboxymethylcellulose 60fold and 16fold, respectively, compared to the wild-type enzyme
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E499A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
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W404A
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site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
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E269S
additional information
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
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the mutant shows 63% increased catalytic activity and stability compared to the wild type enzyme. Half-life values at 60°C and 70°C are 152 and 99 min, respectively
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
the mutant shows increased catalytic activity and stability compared to the wild type enzyme
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
Bacillus tequilensis CGX 5-2
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the mutant shows 63% increased catalytic activity and stability compared to the wild type enzyme. Half-life values at 60°C and 70°C are 152 and 99 min, respectively
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K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
Bacillus tequilensis CGX 5-2
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the mutant shows increased catalytic activity and stability compared to the wild type enzyme
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E119A
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variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
E119A
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variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
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E158A
mutation switches the activity from mainly transglycosylation to beta-1,3-glucanase. Hydrolytic activity toward reduced laminarin is 348.5fold higher than the wild type
E158A
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mutation switches the activity from mainly transglycosylation to beta-1,3-glucanase. Hydrolytic activity toward reduced laminarin is 348.5fold higher than the wild type
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E269S
site-directed mutagenesis, nucleophile replacement, inactive mutant
E269S
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site-directed mutagenesis, nucleophile replacement, inactive mutant
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additional information
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enzyme disruption mutant, no further effects on growth rate of mutant strains, but results in formation of chains of cells. Enzyme gene is able to complement eng1 mutants in Saccharomyces cerevisiae
additional information
the recombinant N-terminal domain has high hydrolytic activity on laminarin. The C-terminal domain of Fra e 9, a cysteine-rich compact structure, is able to bind laminarin
additional information
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plants resistant to infection by Orobanche crenata, enzyme is differently expressed in cells near the penetration point
additional information
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deletion mutant lacking resiudes 72-75 hydrolyzes the mixed-linkgae beta-(1-3)-(1-4)-glucan lichenan 10times more efficiently than wild-type
additional information
deletion mutant lacking resiudes 72-75 hydrolyzes the mixed-linkgae beta-(1-3)-(1-4)-glucan lichenan 10times more efficiently than wild-type
additional information
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an enzyme deletion strain shows decreased activity of acid trehalase
additional information
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a point mutation, that destroys the catalytic activity of the protein, results in a phenotype similar to that of the mutant strain with gene eng2 placed under the control of a repressible promoter. Exogenous addition of purified Eng2 releases the ascospores from asci generated by the eng2+-deficient mutant
additional information
C-terminally truncated enzyme without carbohydrate-binding module, about 40% reduction of activity
additional information
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C-terminally truncated enzyme without carbohydrate-binding module, about 40% reduction of activity
additional information
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engineering of dual-functional hybrid glucanases from a truncated and mutated 1,3-1,4-beta-D-glucanase gene TFsW203F from Fibrobacter succinogenes, and a 1,3-beta-D-glucanase gene TmLam from hyperthermophilic Thermotoga maritima used as target enzymes, by ligating substrate-binding domains (TmB1 and TmB2) and the catalytic domain (TmLamCD) of TmLam to the N- or C-terminus of TFsW203F to create four hybrid enzymes, TmB1-TFsW203F, TFsW203F-TmB2, TmB1-TFsW203F-TmB2 and TFsW203F-TmLamCD, creation of desirable hybrid enzymes with economic benefits for industrial applications. Improved thermal tolerance of the hybrid enzyme TFsW203FTmLamCD, fluorescence and circular dichroism spectrometric analyses, overview. Kinetic properties of mutant hybrid glucanases
additional information
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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engineering of dual-functional hybrid glucanases from a truncated and mutated 1,3-1,4-beta-D-glucanase gene TFsW203F from Fibrobacter succinogenes, and a 1,3-beta-D-glucanase gene TmLam from hyperthermophilic Thermotoga maritima used as target enzymes, by ligating substrate-binding domains (TmB1 and TmB2) and the catalytic domain (TmLamCD) of TmLam to the N- or C-terminus of TFsW203F to create four hybrid enzymes, TmB1-TFsW203F, TFsW203F-TmB2, TmB1-TFsW203F-TmB2 and TFsW203F-TmLamCD, creation of desirable hybrid enzymes with economic benefits for industrial applications. Improved thermal tolerance of the hybrid enzyme TFsW203FTmLamCD, fluorescence and circular dichroism spectrometric analyses, overview. Kinetic properties of mutant hybrid glucanases
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