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3.2.1.73: licheninase

This is an abbreviated version!
For detailed information about licheninase, go to the full flat file.

Word Map on EC 3.2.1.73

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beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose
+ 4 H2O = 5 beta-D-glucopyranose

Synonyms

(1,3)(1,4)-beta-D-glucan-4-glucanohydrolase, (1->3,1->4)-beta-glucanase isoenzyme EII, 1,3-1,4-beta-D-glucan 4-glucanohydrolase, 1,3-1,4-beta-D-glucan glucanohydrolase, 1,3-1,4-beta-D-glucan-4-glucano hydrolase, 1,3-1,4-beta-D-glucanase, 1,3-1,4-beta-glucanase, 1,3;1,4-beta-glucan 4-glucanohydrolase, 1,3;1,4-beta-glucan endohydrolase, Af-EGL7, Afu6g01800, Beg1, beta-(1,3-1,4)-glucanase, beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase, beta-1,3-1,4 glucanase, beta-1,3-1,4-D-glucanase, beta-1,3-1,4-glucanase, beta-1,3;1,4-glucanase, beta-1-3, 1-4 glucan 4-glucanohydrolase, beta-glucanase, BG1, Bg1314, Bga1, bgc, bgi, Bgl, bgl5-1, BglA, BglA13, BglA16, BglA51, BglBB, bglBC1, BGlc8H, BglM2, BglS, BglT, BglTO, Bglu16A, bifunctional xylanase/endoglucanase, BLB369, BLB369 endo-beta-1,3-1,4-glucanase, Blc8H, BP_Cel9A, Cel5F, CP7 beta-1,3-1,4-glucanase, CtGlu16A, Cthe_0211, CtLic16A, CtLic26A, E-LICHN, EG1, EGL, EII, endo-(1,3)(1,4)-beta-glucanase, endo-(1,3;1,4)-beta-glucanase, endo-beta-1,3-1,4 glucanase, endo-beta-1,3-1,4-glucanase, endo-beta-1,3;1,4-glucan-D-glycosyl hydrolase, endo-beta-glucanase, endoglucanase, endotype beta-1,3-1,4-glucanase, Fisuc_2961, Fsbeta-glucanase, FSU_0226, Gcs2, GH7 endo-1,4-beta-glucanase, GHF16 TFsbeta-glucanase, GHF17 barley 1,3-1,4-beta-D-glucanase, Glc16A, GLU-1, GLU-3, glu369, Gluc5_26A, GluIII, GluUS570, glycoside hydrolase family 9 endoglucanase, GyrA, H(A16-M), lam1, LamA, laminarinase, Lic16A, Lic8H, LicA, LicB, Lichenase, lichenase-2, LicKM, licM, LicMB, LicS, McLic1, mHG, Mixed linkage beta-glucanase, More, NFEg16A, PbBglu16A, PlicA, PtLic16A, Ra0505, RuCelA, TaGlu34, TC2, TC5, TF-glu, TF-glucanase, theme C glycoside hydrolase family 9 endo-beta-glucanase, TM1752, US8_01508, XynIII, XynZ, ZgLamA

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.73 licheninase

Engineering

Engineering on EC 3.2.1.73 - licheninase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K142N/Q203L/N214D
E134A
E134A/E138A
-
no enzymic activity, but reaction occurs in presence of sodium azide, E138 is the general acid-base catalyst
N207D
mutant displays better thermotolerance than the wild type but also reduced activity
A98W
-
active-site variant
E105Q/E109Q
-
catalytically impaired
E131Q
-
active-site variant
E63D
-
active-site variant
E63Q
-
active-site variant
H99D
-
active-site variant
K48A
-
123% of wild-type activity, thermostability and halostability are enhanced. Catalytic efficiency of mutants is enhanced as a result of the increase in substrate affinity. The half-lives of the mutant increases up to about 7fold at 60-70°C
K48L
-
137% of wild-type activity, thermostability and halostability are enhanced. Catalytic efficiency of mutants is enhanced as a result of the increase in substrate affinity. The half-lives of the mutant increases up to about 7fold at 60-70°C
N26A
-
active-site variant
R65A
-
active-site variant
S90A
-
active-site variant
W184Y
-
active-site variant
W192A
-
active-site variant
Y123A
-
active-site variant
Y123F
-
active-site variant
Y24A
-
active-site variant
Y24F
-
active-site variant
Y24W
-
active-site variant
K48A
-
123% of wild-type activity, thermostability and halostability are enhanced. Catalytic efficiency of mutants is enhanced as a result of the increase in substrate affinity. The half-lives of the mutant increases up to about 7fold at 60-70°C
-
K48L
-
137% of wild-type activity, thermostability and halostability are enhanced. Catalytic efficiency of mutants is enhanced as a result of the increase in substrate affinity. The half-lives of the mutant increases up to about 7fold at 60-70°C
-
K48A
mutation enhances catalytic efficiency, thermostability and halostability
K48L
mutation enhances catalytic efficiency, thermostability and halostability
M44V/N53H
T113S
mutant displays improved thermal stability
M44V/N53H
T113S
-
mutant displays improved thermal stability
-
E46P/S43E/H205P/S40E
-
64% increase in specific activity, 20°C increase in optimal enzymatic temperature and a 13.8 °C rise in protein melting temperature compared to wild-type
K20S/N31C/S40E/S43E/E46P/P102C/K117S/N125C/K165S/T187C/H205P
mutant with increased catalytic activity and thermostability
N31C/T187C
-
the mutations significantly enhance the protein thermostability
N31C/T187C/P102C/N125C
P102C/N125C
-
the mutations significantly enhance the protein thermostability
E46P/S43E/H205P/S40E
-
64% increase in specific activity, 20°C increase in optimal enzymatic temperature and a 13.8 °C rise in protein melting temperature compared to wild-type
-
N31C/T187C
-
the mutations significantly enhance the protein thermostability
-
N31C/T187C/P102C/N125C
P102C/N125C
-
the mutations significantly enhance the protein thermostability
-
233Stop
28.4% of wild-type activity
D202L
shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
D202N
exhibits a 1.8fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
D206M
shows a 1.1fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
D206N
exhibits a 1.5fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
D206R
exhibits the highest relative activity at 50°C over 10 min, shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
D58A
-
no enzymatic activity
D58E
-
dramatic decrease in kcat, substrate affinity similar to wild type
D58N
-
dramatic decrease in kcat, substrate affinity similar to wild type
E11L
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
E47I
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value
E56A
-
no enzymatic activity
E56D
-
dramatic decrease in kcat, substrate affinity similar to wild type
E56Q
-
no enzymatic activity
E60A
-
no enzymatic activity
E60D
-
dramatic decrease in kcat, substrate affinity similar to wild type
E60Q
-
no enzymatic activity
E85D
has 5fold lower kcat/Km ratios than the wild-type
E85I
has 5fold lower kcat/Km ratios than the wild-type
F205L
shows a 3.8fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
F40I
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, significant decrease in catalytic efficiency
G201S
shows a 1.5fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
G207N
shows a fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
G63A
-
decrease in thermostability
K200F
is the most heat-sensitive enzyme, retains 72% of activity at 45°C for 10 min, shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
K200M
shows a 1.1fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
K64A
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure
K64M
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value
L62G
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure
M27D/M39R
M27R/M39D
N139A
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
N208G
shows a fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
N44L
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure
N44Q
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value
N72A
has 11fold lower kcat/Km ratios than the wild-type
N72Q
has 17fold lower kcat/Km ratios than the wild-type
Q70A
has 299fold lower kcat/Km ratios than the wild-type
Q70D
has 62fold lower kcat/Km ratios than the wild-type
Q70E
has 106fold lower kcat/Km ratios than the wild-type
Q70I
has 499fold lower kcat/Km ratios than the wild-type
Q70N
has 63fold lower kcat/Km ratios than the wild-type
Q70R
has 35fold lower kcat/Km ratios than the wild-type
Q81I
has 2fold lower kcat/Km ratios than the wild-type
Q81N
has 2.5fold lower kcat/Km ratios than the wild-type
R137M
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
R137Q
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
R209M
shows a 1.1fold increase, in catalytic efficiency (kcat/KM) compared to the wild-type
T204F
shows a 2.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
V18Y/W203Y
W105F
-
significant decrease in thermostability
W105H
-
significant decrease in thermostability
W141F
-
5-7-fold increase in KM-value for lichenan compared to wild type, decrease in kcat-value, no significant change in thermal stability
W141H
-
5-7-fold increase in KM-value for lichenan compared to wild type, decrease in kcat-value, no significant change in thermal stability
W148F
-
decrease in kcat-value, no significant change in thermal stability
W165F
-
after incubation at pH 3.0, 1 h, 3-7-fold higher activity than wild type
W165H
-
significant decrease in thermostability
W186F
-
increase in kcat-value, no significant change in thermal stability
W198F
-
significant decrease in thermostability
W203F
W203R
W203Y
W54F
-
decrease in kcat-value, no significant change in thermal stability
W54Y
-
decrease in kcat-value, no significant change in thermal stability
Y42L
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity
A79P
-
decrease in thermal stability
F85Y
-
decrease in thermal stability
G44R
-
decrease in thermal stability
H300P
-
increase in thermal stability
K23R
-
decrease in thermal stability
M298K
-
thermal stabiltiy similar to wild type
N290H
-
slight increase in thermal stability
D70V
-
thermostable mutant, similar katalytic efficiency as wild type
C263S
-
random mutagenesis, the mutant shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme
D221G2
-
random mutagenesis, the mutant shows unaltered properties compared to the wild-type enzyme
D56G
-
random mutagenesis, the mutant shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme
D56G/D221G/C263S
-
random mutagenesis, mutant PtLic16AM2 shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme. Mutation D221G alone does not lead to altered enzyme properties
E113A
-
inactive mutant. In the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration
W108A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E113A
inactive mutant. In the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration
W108A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E113A
-
inactive mutant. In the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration
-
W108A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
W108F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
W108Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
W253A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
D105K
-
activity is reduced to less than 1%
D105N
-
activity is reduced to less than 1%
E103D
-
activity is reduced to less than 1%
E103Q
-
activity is reduced to less than 1%
E107D
-
activity is reduced to less than 1%
E107H
-
activity is reduced to less than 1%
E107Q
-
activity is reduced to less than 1%
W101F
-
activity is reduced to less than 1%
W101Y
-
activity is reduced to less than 1%
D100A
-
36% relative activity compared to the wild type enzyme
D106A
-
34% relative activity compared to the wild type enzyme
D195A
-
36% relative activity compared to the wild type enzyme
D220A
-
32% relative activity compared to the wild type enzyme
D258A
-
35% relative activity compared to the wild type enzyme
D314A
-
99% relative activity compared to the wild type enzyme
D317A
-
31% relative activity compared to the wild type enzyme
E196A
-
39% relative activity compared to the wild type enzyme
E222A
-
no activity
E242A
-
32% relative activity compared to the wild type enzyme
E262A
-
36% relative activity compared to the wild type enzyme
E323A
-
32% relative activity compared to the wild type enzyme
E91A
-
no activity
D195A
-
36% relative activity compared to the wild type enzyme
-
D258A
-
35% relative activity compared to the wild type enzyme
-
D314A
-
99% relative activity compared to the wild type enzyme
-
E222A
-
no activity
-
E323A
-
32% relative activity compared to the wild type enzyme
-
D156A
almost complete loss of activity
Q95A
almost complete loss of activity
C17R/Q87T/D152G/Y307H/V330A/N344D
E149D/V370E
the mutant shows 59.9% activity at pH 5.5 and 50°C compared to the wild type enzyme
K12R/F30L/N114D/N252D/T348S/N380S
the mutant shows 62.1% activity at pH 5.5 and 50°C compared to the wild type enzyme
N197D/M322V
N4S
the mutant shows 75.3% activity at pH 5.5 and 50°C compared to the wild type enzyme
S11R/T210S
the mutant shows 231.3% activity at pH 5.5 and 50°C compared to the wild type enzyme
Y389F/ K395R
the mutant shows 81% activity at pH 5.5 and 50°C compared to the wild type enzyme
E269S
additional information