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3.2.1.91: cellulose 1,4-beta-cellobiosidase (non-reducing end)

This is an abbreviated version!
For detailed information about cellulose 1,4-beta-cellobiosidase (non-reducing end), go to the full flat file.

Word Map on EC 3.2.1.91

Reaction

2 cellohexaose + 2 H2O = 2 cellotriose +

cellotetraose
+
cellobiose

Synonyms

1,4-beta-cellobiohydrolase, 1,4-beta-D-glucan cellobiohydrolase, 1,4-beta-glucan cellobiohydrolase, 1,4-beta-glucan cellobiosidase, avicelase, avicelase II, beta-1,4-glucan cellobiohydrolase, beta-1,4-glucan cellobiosylhydrolase, beta-1,4-glycanase, Beta-1,4-glycanase CEX, Beta-glucancellobiohydrolase, C1 cellulase, CBH, CBH 1, Cbh C, CBH I, CBH Ib, CBH II, CBH IIb, CBH1, CBH2, Cbh6B, Cbh9A, CbhA, CBHI, CBHII, Cbhl.2, CBM3-GH5, CBP120, CBP95, CbsA, Cel5A, Cel6, Cel6A, Cel6B, Cel6C, Cel7A, Cel7D, CelA, CelAB, CelB, CelC7, CelK, cellobiohydrolase, cellobiohydrolase 1, cellobiohydrolase 9A, cellobiohydrolase A, cellobiohydrolase class II, cellobiohydrolase I, cellobiohydrolase II, cellobiohydrolase, exo-, cellobiosidase, cellobiosidase, 1,4-beta-glucan, Celluclast 1.5, Cellulase, cellulase, C1, Cex, Csac_1078, Ex-1, Ex-4, exo-1,4-beta-D-glucan cellobiohydrolase, exo-1,4-beta-D-glucanase, exo-beta-1,4-cellobiohydrolase, exo-beta-1,4-glucan cellobiohydrolase, exo-cellobiohydrolase, exocellobiohydrolase, exocellulase, exocellulase E3, exoglucanase, GH5, glucanase, Huta_2387, More, nonreducing end-acting cellobiohydrolase, oligosaccharide-specific cellobiohydrolase, PSCase, SCO6546, Ta Cel7A, THITE_126432, TTCBH6B

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.91 cellulose 1,4-beta-cellobiosidase (non-reducing end)

Engineering

Engineering on EC 3.2.1.91 - cellulose 1,4-beta-cellobiosidase (non-reducing end)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D262A
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
D264A
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
T230A
site-directed mutagenesis, mutation of the module interface residue affects the final fold and stability of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
T230A/D262A
site-directed mutagenesis, mutation of the residues affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
W678G
the binding free energies between the substrate and the mutant are higher than those of the wild type enzyme. The pull forces and energy barrier in the mutant is also reduced significantly
Y555S
the binding free energies between the substrate and the mutant are higher than those of the wild type enzyme. The pull forces and energy barrier in the mutant is also reduced significantly
D262A
-
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
-
D264A
-
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
-
T230A
-
site-directed mutagenesis, mutation of the module interface residue affects the final fold and stability of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
-
T230A/D262A
-
site-directed mutagenesis, mutation of the residues affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
-
A385P
-
the mutant shows a T50 value of 64.7°C
C313S
random mutagenesis, the mutation causes increased thermostability of the mutant enzyme compared to the wild-type, with decreased inactivation, increased maximum Avicel hydrolysis temperature, and improved long time hydrolysis performance
D405A
about 1% enzyme activity
D405N
only small structural changes, about 1% enzyme activity
D416A
M235P
-
the mutant shows a T50 value of 63.1°C
Q390P
-
the mutant shows a T50 value of 66.1°C
S215P
-
the mutant shows a T50 value of 65.6°C
C313S
-
random mutagenesis, the mutation causes increased thermostability of the mutant enzyme compared to the wild-type, with decreased inactivation, increased maximum Avicel hydrolysis temperature, and improved long time hydrolysis performance
A401P
-
the mutant enzyme shows improved thermostability compared to the wild type enzyme
A426P
-
the mutant shows 86.9% of wild type activity
S273P
-
the mutant enzyme shows improved thermostability compared to the wild type enzyme
S298P
-
the mutant shows 88% of wild type activity
T237G
-
the mutant enzyme shows improved thermostability compared to the wild type enzyme
T262G
-
the mutant shows 94.4% of wild type activity
T262G /S298P /A426P
-
the mutant shows 95.7% of wild type activity
D226A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme. The D226A enzyme has a very low activity on insoluble cellulose, not improved by sodium azide
D226A/S232A
-
site-directed mutagenesis, the mutant is almost inactive and shows slightly decreased ligand binding compared to the wild-type enzyme
D274A
-
site-directed mutagenesis, the mutant shows altered and highly reduced substrate specificity compared to the wild-type enzyme
D497A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
D512A
-
site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
E495A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
L230A
-
site-directed mutagenesis, the mutation causes slightly increased processivity and increased activity with phosphoric acid-treated cotton over 250%, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
M514A
-
site-directed mutagenesis, the mutation alters the secondary structure of the enzyme, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
M514Q
-
site-directed mutagenesis, the mutation alters the secondary structure of the enzyme, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
N282A
-
site-directed mutagenesis, mutation in residue near the tunnel entrance causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
N282D
-
site-directed mutagenesis, mutation in residue near the tunnel entrance causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
R180A
-
site-directed mutagenesis, mutation in residue near the tunnel exit causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
R180K
-
site-directed mutagenesis, mutation in residue near the tunnel exit causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
S232A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme. The S232A enzyme retains near wild-type activity on most substrates, but carboxymethylcellulose activity is drastically reduced
W464A
-
site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
W464Y
-
site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
Y220A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme, alomost inactive mutant
S131W
Thermochaetoides thermophila
the mutant with reduced activity exhibits effectively enhanced heat resistance to elevated temperatures. The half-life of this mutant enzyme is increased 1.42 and 2.40fold at 80°C and 90°C, respectively, compared to the wild type
W221R
Thermochaetoides thermophila
the mutant shows significantly declined activity compared to the wild type enzyme
W315R
Thermochaetoides thermophila
the mutant shows significantly declined activity compared to the wild type enzyme
Y119F
Thermochaetoides thermophila
the mutation increases the catalytic activity 1.82, 1.65 and 1.43fold against beta-D-glucan, phosphoric acid swollen cellulose and carboxymethyl cellulose, respectively, compared to the wild type enzyme
S131W
Thermochaetoides thermophila DSM 1495
-
the mutant with reduced activity exhibits effectively enhanced heat resistance to elevated temperatures. The half-life of this mutant enzyme is increased 1.42 and 2.40fold at 80°C and 90°C, respectively, compared to the wild type
-
W221R
Thermochaetoides thermophila DSM 1495
-
the mutant shows significantly declined activity compared to the wild type enzyme
-
W315R
Thermochaetoides thermophila DSM 1495
-
the mutant shows significantly declined activity compared to the wild type enzyme
-
Y119F
Thermochaetoides thermophila DSM 1495
-
the mutation increases the catalytic activity 1.82, 1.65 and 1.43fold against beta-D-glucan, phosphoric acid swollen cellulose and carboxymethyl cellulose, respectively, compared to the wild type enzyme
-
Y466A
the mutation greatly reduces the cellulose-binding ability
Y492A
the mutation greatly reduces the cellulose-binding ability
Y493A
the mutation greatly reduces the cellulose-binding ability
C313S
random mutagenesis, the mutation causes increased thermostability of the mutant enzyme compared to the wild-type, with decreased inactivation, increased maximum Avicel hydrolysis temperature, and improved long time hydrolysis performance. The C313S mutation increases total Humicola jecorina CBH II activity secreted by the Saccharomyces cerevisiae expression host more than 10fold
D175A
mutant retains some activity on longer oligosaccharides
D221A
almost complete loss of activity
D241C/D249C
thermostability similar to wild-type enzyme
DELTAG245-Y252
reduced thermostability
E107Q
mutant enzyme is destabilized at acidic pH and stabilized at alkaline pH
E107Q/D170N/D366N
mutant enzyme is destabilized at acidic pH and stabilized at alkaline pH
E212Q
site-directed mutagenesis, catalytic residue, inactive mutant
E217Q
site-directed mutagenesis, catalytic residue, inactive mutant
M134L
-
the mutant shows a T50 value of 62°C
Q276L
-
the mutant shows a T50 value of 58.6°C
S30F
-
the mutant shows a T50 value of 60.3°C
S316P
-
the mutant shows a T50 value of 61.9°C
S406P
-
the mutant shows a T50 value of 61.5°C
S413P
-
the mutant shows a T50 value of 63.8°C
W272A
-
mutant
W272D
-
mutant
Y169F
-
mutant
Y247F
slight reduction of kcat on 4-nitrophenyl lactoside, but only a small effect on cellulose hydrolysis
Y31A
-
structural role minor, but does not bind strongly to cellulose
Y32A
-
structural role minor, but does not bind strongly to cellulose
Y5A
-
complete loss of binding affinity to cellulose
W272A
-
mutant
-
W272D
-
mutant
-
Y169F
-
mutant
-
D131A
additional information