3.2.1.73: licheninase This is an abbreviated version! For detailed information about licheninase, go to the full flat file .
Reaction
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
Inhibitors
Inhibitors on EC 3.2.1.73 - licheninase
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(3,4)-epoxybutyl beta-D-cellobioside
-
identification of Glu105 at the active site
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
-
2,4,6-Trinitrobenzenesulfonic acid
Thermomonospora sp.
-
-
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
5,5'-dithiobis 2-nitrobenzoic acid
Thermomonospora sp.
-
-
Al3+
35% inhibition at 10 mM
beta-mercaptoethanol
-
inhibits the enzyme activity at 4 mM by 82.7%
CaCl2
-
10 mM, 33% inhibition
dithiothreitol
-
1 mM, 21% inhibition
EGTA
10 mM, 24% inhibition
epoxyalkyl cellobiosides
-
Glc-beta-1,3-isofagomine
-
-
glucono-delta-lactone
-
-
H2O2
-
at 0.5% w/v hydrogen peroxide, isozymes EG1 and EG2 retain 82.8% and 90.28% of their activities, respectively. At 1% w/v hydrogen peroxide, isozyme EG2 retains 60% activity, while isozyme EG1 is completely inhibited
hexadecyltrimethylammonium bromide
-
1 mM, no residual activity
N-bromosuccinimide
-
1 mM, no residual activity
Na+
-
inhibits the enzyme activity at 4 mM by 47.3%; inhibits the enzyme activity at 4 mM by 80.3%
NaCl
-
30%, halflife of wild-type 230 h, mutant K48A 694 h, mutant K48L 693 h, respectively
Ni2+
-
inhibits the enzyme activity at 4 mM by 11.5%
o-phthaldehyde
Thermomonospora sp.
-
-
Sodium dodecyl sulfate
strong inhibition
sodium perborate
-
isozymes EG1 and EG2 retain 58% and 66.8% of their activities after 1 h of incubation at 40°C in the presence of 0.2% w/v sodium perborate, respectively
Sr2+
-
inhibits the enzyme activity at 4 mM by 49%
Urea
-
14.5% residual activity at 7 mM
2-mercaptoethanol
-
10 mM, 28% inhibition
2-mercaptoethanol
0.5%, 42% residual activity
2-mercaptoethanol
-
inhibits activity at a concentration of 5%
Ag+
complete inhibition at 5 mM
Ag+
-
inhibits the enzyme activity at 4 mM by 56.9%
Ag+
-
12.9% residual activity at 1 mM; strong inhibition
Ba2+
-
8% inhibition at 1 mM
Ba2+
18% inhibition at 10 mM
Ca2+
-
90.98% residual activity at 1 mM
Ca2+
-
11% inhibition at 5 mM
Ca2+
-
partially inhibited
Ca2+
16% inhibition at 10 mM, 15% at 1 mM
Ca2+
1 mM, 74% residual activity
Ca2+
-
inhibits the enzyme activity at 4 mM by 55.5%
Ca2+
-
78.65% residual activity at 1 mM
Co2+
-
82.19% residual activity at 1 mM
Co2+
-
52% inhibition at 5 mM
Co2+
-
inhibits isozyme EG1 by 35%, and isozyme EG2 also slightly, at 2.5 mM
Co2+
5 mM, 50% residual activity
Co2+
6% inhibition at 10 mM, 16% at 1 mM
Co2+
-
40% inhibition at 5 mM
Co2+
43% inhibition at 10 mM
Cu2+
-
inhibits 37% at 10 mM
Cu2+
32.4% inhibition at 5 mM
Cu2+
-
44% residual activity at 1 mM
Cu2+
-
complete inhibition at 5 mM
Cu2+
-
inhibits isozyme EG1 by 28%, but slightly activates isozyme EG2 at 2.5 mM
Cu2+
-
partially inhibited
Cu2+
10 mM, wild-type, complete loss of activity
Cu2+
-
14% inhibition at 1 mM
Cu2+
-
completely inhibits the enzyme activity at 4 mM
Cu2+
-
40% inhibition at 5 mM
Cu2+
-
91.01% residual activity at 0.5 mM
Cu2+
35% inhibition at 10 mM
DTT
-
DTT
-
inhibits the enzyme activity at 4 mM by 82.3%
EDTA
-
10 mM, 18% inhibition
EDTA
-
79.64% residual activity at 1 mM
EDTA
-
1 mM, 77% residual activity
EDTA
10 mM, wild-type, 86% residual activity
EDTA
0.5%, 51% residual activity
EDTA
-
12% inhibition at 1 mM
EDTA
-
inhibits the enzyme activity at 4 mM by 43.4%
EDTA
-
52% inhibition at 5 mM
EDTA
-
47.3% residual activity at 60 mM
EDTA
5 or 10 mM of EDTA reduce barley beta-glucan hydrolysis by 39% and 34%, respectively
epoxyalkyl cellobiosides
-
irreversible active-site directed inactivation, stereospecific requirements for inhibition
-
epoxyalkyl cellobiosides
-
irreversible active-site directed inactivation, stereospecific requirements for inhibition
-
Fe2+
-
inhibits 51% at 10 mM
Fe2+
-
complete inhibition at 5 mM
Fe2+
-
inhibits isozyme EG1 by 50% at 2.5 mM
Fe2+
-
slightly inhibited
Fe2+
92% inhibition at 10 mM
Fe2+
-
inhibits the enzyme activity at 4 mM by 14.9%
Fe2+
-
84.27% residual activity at 1 mM
Fe3+
-
1 mM, 65% residual activity
Fe3+
-
5 mM, 58% of initial activity
Fe3+
1 mM, 9% residual activity
Fe3+
-
inhibits the enzyme activity at 4 mM by 13.5%
Fe3+
-
93.26% residual activity at 1 mM
Fe3+
complete inhibition at 10 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
complete inhibition of both isozymes at 2.5 mM
Hg2+
1 mM, 36% residual activity
Hg2+
-
completely inhibits the enzyme activity at 4 mM
Hg2+
-
14.7% residual activity at 1 mM; strong inhibition
Hg2+
-
complete inhibition at 5 mM
Hg2+
-
complete inhibition
Hg2+
complete inhibition at 10 mM
K+
-
95.61% residual activity at 1 mM
K+
15% inhibition at 10 mM
Li+
48.5% inhibition at 10 mM, 18% at 1 mM
Li+
1 mM, 80% residual activity
Li+
-
66.29% residual activity at 0.5 mM
Li+
8.5% inhibition at 10 mM
Mg2+
5 mM, 84% residual activity
Mg2+
-
slightly inhibited
Mg2+
activates by 89% at 1 mM, inhibits 50% at 10 mM
Mg2+
-
8% inhibition at 1 mM
Mg2+
-
inhibits the enzyme activity at 4 mM by 52.9%
Mg2+
-
90% inhibition at 5 mM
Mg2+
-
78.65% residual activity at 0.5 mM
Mg2+
12% inhibition at 10 mM
Mn2+
-
inhibits 6.5% at 10 mM
Mn2+
activates by 233% at 5 mM, best at 10 mM, slightly inhibitory at 20 mM
Mn2+
-
37.29% residual activity at 1 mM
Mn2+
-
complete inhibition at 5 mM
Mn2+
-
1 mM, 87% residual activity
Mn2+
5 mM, 25% residual activity
Mn2+
-
partially inhibited
Mn2+
10 mM, wild-type, 36% residual activity
Mn2+
45% inhibition at 10 mM, 20% at 1 mM
Mn2+
-
67% inhibition at 1 mM
Mn2+
-
completely inhibits the enzyme activity at 4 mM
Mn2+
-
complete inhibition at 5 mM
Mn2+
-
77.53% residual activity at 1 mM
Pb2+
-
79.29% residual activity at 1 mM
Pb2+
-
97.75% residual activity at 0.5 mM
SDS
-
100 mM, 28% inhibition
SDS
-
the strong anionic surfactant at 0.1% and 0.5% causes a moderate inhibition of 27.5% and 30.7% of isozyme EG2 activity. Isozyme EG1 is highly stable against SDS and retains 100% of its activity in the presence of 0.1% and 0.5% SDS
SDS
-
1 mM, no residual activity
SDS
-
inhibits the enzyme activity at 4 mM by 88.2%
SDS
-
inhibits activity at a concentration of 5%
SDS
14% inhibition at 10 mM
Zn2+
-
inhibits 15% at 10 mM
Zn2+
20.4% inhibition at 5 mM
Zn2+
-
88.66% residual activity at 1 mM
Zn2+
-
78% inhibition of isozyme EG1, poor inhibition of isozyme EG2
Zn2+
-
1 mM, 87% residual activity
Zn2+
-
partially inhibited
Zn2+
52% inhibition at 10 mM, 44% at 1 mM
Zn2+
-
8% inhibition at 1 mM
Zn2+
-
inhibits the enzyme activity at 4 mM by 11.6%
Zn2+
-
complete inhibition at 5 mM
Zn2+
-
69.66% residual activity at 0.5 mM
Zn2+
73% inhibition at 10 mM
additional information
-
poor inhibition at 10 mM by Co2+ and EDTA
-
additional information
-
no significant effects are found for Ca2+, Mg2+, glycerol, D-sorbitol, boric acid, and EDTA
-
additional information
-
the isozymes are highly stable in the presence of non-ionic surfactants such as Tween 80 and Triton X-100
-
additional information
not inhibitory: EDTA at 5 mM
-
additional information
-
not inhibitory: EDTA at 5 mM
-
additional information
-
not inhibited by Li+; not inhibited by Li+, not significantly by Fe2+
-
additional information
-
not inhibitory: EDTA
-
additional information
-
no inhibition up to a concentration of 10% SDS-PAGE
-
additional information
-
resistent to trypsin protease digestion
-
additional information
-
no inhibition by Ca2+ and Fe2+ at 1 mM
-
additional information
-
substrate inhibition for 4-methylumbelliferyl laminaribiose, but not for 4-methylumbelliferyl cellobiose
-
additional information
KM079629
poor inhibition by Fe3+
-