Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Hua, C.; Li, W.; Han, W.; Wang, Q.; Bi, P.; Han, C.; Zhu, L.
    Characterization of a novel thermostable GH7 endoglucanase from Chaetomium thermophilum capable of xylan hydrolysis (2018), Int. J. Biol. Macromol., 117, 342-349 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.4 industry the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively Thermochaetoides thermophila
3.2.1.8 industry the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively Thermochaetoides thermophila

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.4 gene ctendo7, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of C-terminally His6-tagged enzyme in Pichia pastoris strain GS115 Thermochaetoides thermophila
3.2.1.4 heterologously expressed in Pichia pastoris Thermochaetoides thermophila
3.2.1.8 gene ctendo7, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of C-terminally His6-tagged enzyme in Pichia pastoris strain GS115 Thermochaetoides thermophila
3.2.1.8 heterologously expressed in Pichia pastoris Thermochaetoides thermophila

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.4 Ag+ 23% inhibition at 1 mM, 68% inhibition at 5 mM; 5 mM, 62.5% loss of activity, substrate: xylan; 5 mM, 68.25% loss of activity, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.4 Co2+ 5 mM, 2% loss of activity, substrate: xylan Thermochaetoides thermophila
3.2.1.4 Cu2+ 5 mM, complete loss of activity, substrate: carboxymethyl cellulose; 5 mM, complete loss of activity, substrate: xylan; 75% inhibition at 1 mM, complete inhibition at 5 mM Thermochaetoides thermophila
3.2.1.4 Fe3+ 14% inhibition at 1 mM, 70% inhibition at 5 mM; 5 mM, 70.3% loss of activity, substrate: carboxymethyl cellulose; 5 mM, 78.5% loss of activity, substrate: xylan Thermochaetoides thermophila
3.2.1.4 Mg2+ 5 mM, 51% loss of activity, substrate: xylan; 5 mM, 64.5% loss of activity, substrate: carboxymethyl cellulose; 6% inhibition at 1 mM, 64.5% inhibition at 5 mM Thermochaetoides thermophila
3.2.1.4 Zn2+ 5 mM, 4.4% loss of activity, substrate: carboxymethyl cellulose; 5 mM, 55% loss of activity, substrate: xylan Thermochaetoides thermophila
3.2.1.8 Ag+ 18.5% inhibition at 1 mM, 62.5% inhibition at 5 mM; 5 mM, 62.5% loss of activity, substrate: xylan; 5 mM, 68.25% loss of activity, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.8 Co2+ 5 mM, 2% loss of activity, substrate: xylan Thermochaetoides thermophila
3.2.1.8 Cu2+ 5 mM, complete loss of activity, substrate: carboxymethyl cellulose; 5 mM, complete loss of activity, substrate: xylan; complete inhibition at 1-5 mM Thermochaetoides thermophila
3.2.1.8 Fe3+ 5 mM, 70.3% loss of activity, substrate: carboxymethyl cellulose; 5 mM, 78.5% loss of activity, substrate: xylan; 8.3% inhibition at 1 mM, 78.5% inhibition at 5 mM Thermochaetoides thermophila
3.2.1.8 Mg2+ 22.7% inhibition at 1 mM, 50.6% inhibition at 5 mM; 5 mM, 51% loss of activity, substrate: xylan; 5 mM, 64.5% loss of activity, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.8 Zn2+ 17.1% inhibition at 1 mM, 55.2% at 5 mM; 5 mM, 4.4% loss of activity, substrate: carboxymethyl cellulose; 5 mM, 55% loss of activity, substrate: xylan Thermochaetoides thermophila

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.4 additional information
-
 beta-1,4-D-xylan Km-value: 10.28 mg/ml, pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.4 additional information
-
 carboxymethyl cellulose Km-value: 79.19 mg/ml, pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.4 additional information
-
 beta-1,4-D-glucan Km-value: 9.82 mg/ml, pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.4 additional information
-
 additional information Michaelis-Menten kinetics, Km is 9.82 mg/ml for barley beta-1,4-D-glucan Thermochaetoides thermophila
3.2.1.8 additional information
-
 beta-1,4-D-xylan Km-value: 10.28 mg/ml, pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.8 additional information
-
 carboxymethyl cellulose Km-value: 79.19 mg/ml, pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.8 additional information
-
 beta-1,4-D-glucan Km-value: 9.82 mg/ml, pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.8 additional information
-
 additional information Michaelis-Menten kinetics, Km is 10.28 mg/ml for beta-1,4-D-xylan Thermochaetoides thermophila

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.4 Ca2+ 5 mM, 1.1fold activation, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.4 Ca2+ 5 mM, 1.2fold activation, substrate: xylan Thermochaetoides thermophila
3.2.1.4 Co2+ 5 mM, 1.4fold activation, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.4 Co2+ activates at 1-5 mM Thermochaetoides thermophila
3.2.1.4 Mn2+ 5 mM, 1.4fold activation, substrate: xylan Thermochaetoides thermophila
3.2.1.4 Mn2+ 5 mM, 1.7fold activation, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.4 Mn2+ activates at 1-5 mM Thermochaetoides thermophila
3.2.1.4 additional information poor effects by Ca2+ on endoglucanase activity at 1-5 mM Thermochaetoides thermophila
3.2.1.4 Zn2+ activates at 1 mM, slight inhibition at 5 mM Thermochaetoides thermophila
3.2.1.8 Ca2+ 5 mM, 1.1fold activation, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.8 Ca2+ 5 mM, 1.2fold activation, substrate: xylan Thermochaetoides thermophila
3.2.1.8 Ca2+ activates 19.5% at 5 mM Thermochaetoides thermophila
3.2.1.8 Co2+ 5 mM, 1.4fold activation, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.8 Mn2+ 5 mM, 1.4fold activation, substrate: xylan Thermochaetoides thermophila
3.2.1.8 Mn2+ 5 mM, 1.7fold activation, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.8 Mn2+ activates at 47.5% at 1 mM, 38.6% at 5 mM Thermochaetoides thermophila
3.2.1.8 additional information poor effects by 1-5 mM Co2+ Thermochaetoides thermophila

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.4 47000
-
 calculated from sequence Thermochaetoides thermophila
3.2.1.8 47000
-
 calculated from sequence Thermochaetoides thermophila

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.4 Thermochaetoides thermophila G0S9G3
-
-
3.2.1.4 Thermochaetoides thermophila CBS 144.50 G0S9G3
-
-
3.2.1.4 Thermochaetoides thermophila DSM 1495 G0S9G3
-
-
3.2.1.4 Thermochaetoides thermophila IMI 039719 G0S9G3
-
-
3.2.1.8 Thermochaetoides thermophila G0S9G3
-
-
3.2.1.8 Thermochaetoides thermophila CBS 144.50 G0S9G3
-
-
3.2.1.8 Thermochaetoides thermophila DSM 1495 G0S9G3
-
-
3.2.1.8 Thermochaetoides thermophila IMI 039719 G0S9G3
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.4 glycoprotein
-
 Thermochaetoides thermophila
3.2.1.4 glycoprotein predicted one N-linked glycosylation site (N261) and three O-linked glycosylation sites (T32, T312 and T332), respectively Thermochaetoides thermophila
3.2.1.8 glycoprotein
-
 Thermochaetoides thermophila
3.2.1.8 glycoprotein predicted one N-linked glycosylation site (N261) and three O-linked glycosylation sites (T32, T312 and T332), respectively Thermochaetoides thermophila

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.4
-
 Thermochaetoides thermophila
3.2.1.4 recombinant His-tagged enzyme from Pichia pastoris strain GS115 by nickel affinity chromatography Thermochaetoides thermophila
3.2.1.8
-
 Thermochaetoides thermophila
3.2.1.8 recombinant His-tagged enzyme from Pichia pastoris strain GS115 by nickel affinity chromatography Thermochaetoides thermophila

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.4 2.22
-
 purified recombinant His-tagged enzyme, pH 5.0, 55°C, substrate beta-glucan Thermochaetoides thermophila
3.2.1.8 3.05
-
 purified recombinant His-tagged enzyme, pH 5.0, 55°C, substrate beta-xylan Thermochaetoides thermophila

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.4 barley beta-1,4-D-glucan + H2O best endoglucanase substrate Thermochaetoides thermophila ?
-
 ?
3.2.1.4 beta-1,4-D-glucan + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila ?
-
 ?
3.2.1.4 beta-1,4-D-xylan + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila ?
-
 ?
3.2.1.4 carboxymethyl cellulose + H2O 1% w/v CMC-Na Thermochaetoides thermophila ?
-
 ?
3.2.1.4 carboxymethyl cellulose + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila ?
-
 ?
3.2.1.4 additional information the bifunctional enzyme also shows endoxylanase activity (EC 3.2.1.8) hydrolyzing beta-1,4-D-xylan from beechwood. Substrate specificity, overview. No endoglucanase activity on (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose. The enzyme shows activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively Thermochaetoides thermophila ?
-
 ?
3.2.1.8 beta-1,4-D-glucan + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila ?
-
 ?
3.2.1.8 beta-1,4-D-glucan + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila IMI 039719 ?
-
 ?
3.2.1.8 beta-1,4-D-glucan + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila DSM 1495 ?
-
 ?
3.2.1.8 beta-1,4-D-glucan + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila CBS 144.50 ?
-
 ?
3.2.1.8 beta-1,4-D-xylan + H2O 0.5% w/v xylan from beechwood Thermochaetoides thermophila ?
-
 ?
3.2.1.8 beta-1,4-D-xylan + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila ?
-
 ?
3.2.1.8 beta-1,4-D-xylan + H2O 0.5% w/v xylan from beechwood Thermochaetoides thermophila IMI 039719 ?
-
 ?
3.2.1.8 beta-1,4-D-xylan + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila IMI 039719 ?
-
 ?
3.2.1.8 beta-1,4-D-xylan + H2O 0.5% w/v xylan from beechwood Thermochaetoides thermophila DSM 1495 ?
-
 ?
3.2.1.8 beta-1,4-D-xylan + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila DSM 1495 ?
-
 ?
3.2.1.8 beta-1,4-D-xylan + H2O 0.5% w/v xylan from beechwood Thermochaetoides thermophila CBS 144.50 ?
-
 ?
3.2.1.8 beta-1,4-D-xylan + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila CBS 144.50 ?
-
 ?
3.2.1.8 carboxymethyl cellulose + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila ?
-
 ?
3.2.1.8 carboxymethyl cellulose + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila IMI 039719 ?
-
 ?
3.2.1.8 carboxymethyl cellulose + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila DSM 1495 ?
-
 ?
3.2.1.8 carboxymethyl cellulose + H2O bifunctional endoglucanase/xylanase enzyme Thermochaetoides thermophila CBS 144.50 ?
-
 ?
3.2.1.8 additional information the bifunctional enzyme also shows endoglucanase activity (EC 3.2.1.4) hydrolyzing carboxymethyl cellulose and barley beta-glucan. Substrate specificity, overview. The enzyme shows endoglucanase, but not xylanase, activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively. No xylanase activity with (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose Thermochaetoides thermophila ?
-
 ?
3.2.1.8 additional information the bifunctional enzyme also shows endoglucanase activity (EC 3.2.1.4) hydrolyzing carboxymethyl cellulose and barley beta-glucan. Substrate specificity, overview. The enzyme shows endoglucanase, but not xylanase, activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively. No xylanase activity with (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose Thermochaetoides thermophila IMI 039719 ?
-
 ?
3.2.1.8 additional information the bifunctional enzyme also shows endoglucanase activity (EC 3.2.1.4) hydrolyzing carboxymethyl cellulose and barley beta-glucan. Substrate specificity, overview. The enzyme shows endoglucanase, but not xylanase, activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively. No xylanase activity with (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose Thermochaetoides thermophila DSM 1495 ?
-
 ?
3.2.1.8 additional information the bifunctional enzyme also shows endoglucanase activity (EC 3.2.1.4) hydrolyzing carboxymethyl cellulose and barley beta-glucan. Substrate specificity, overview. The enzyme shows endoglucanase, but not xylanase, activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively. No xylanase activity with (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose Thermochaetoides thermophila CBS 144.50 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.4 ? x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE Thermochaetoides thermophila
3.2.1.8 ? x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE Thermochaetoides thermophila

Synonyms

EC Number Synonyms Comment Organism
3.2.1.4 bifunctional endoglucanase/xylanase
-
 Thermochaetoides thermophila
3.2.1.4 ctendo7
-
 Thermochaetoides thermophila
3.2.1.4 CTHT_0045780 gene name, UniProt Thermochaetoides thermophila
3.2.1.4 GH7 endoglucanase
-
 Thermochaetoides thermophila
3.2.1.4 More cf. EC 3.2.1.8 Thermochaetoides thermophila
3.2.1.8 bifunctional endoglucanase/xylanase
-
 Thermochaetoides thermophila
3.2.1.8 ctendo7
-
 Thermochaetoides thermophila
3.2.1.8 CTHT_0045780 gene name, UniProt Thermochaetoides thermophila
3.2.1.8 GH7 endoglucanase
-
 Thermochaetoides thermophila
3.2.1.8 More cf. EC 3.2.1.4 Thermochaetoides thermophila

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.4 55
-
-
 Thermochaetoides thermophila
3.2.1.4 55
-
 for CTendo7's xylanase activity and endoglucanase activity Thermochaetoides thermophila
3.2.1.8 55
-
-
 Thermochaetoides thermophila
3.2.1.8 55
-
 for CTendo7's xylanase activity and endoglucanase activity Thermochaetoides thermophila

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.4 30 90 activity range, profile overview Thermochaetoides thermophila
3.2.1.4 40 80 40°C: about 40% of maximal activity, 80°C: about 50% of maximal activity, substrate: xylan Thermochaetoides thermophila
3.2.1.4 40 80 40°C: about 50% of maximal activity, 80°C: about 50% of maximal activity, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.8 30 90 activity range, profile overview Thermochaetoides thermophila
3.2.1.8 40 80 40°C: about 40% of maximal activity, 80°C: about 50% of maximal activity, substrate: xylan Thermochaetoides thermophila
3.2.1.8 40 80 40°C: about 50% of maximal activity, 80°C: about 50% of maximal activity, substrate: carboxymethyl cellulose Thermochaetoides thermophila

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.4 60
-
 120 min, enzyme retains about 85% of its initial activity, xylanase ativity Thermochaetoides thermophila
3.2.1.4 60
-
 120 min, enzyme retains more than 80% of its initial activity, endoglucanase activity Thermochaetoides thermophila
3.2.1.4 60
-
 purified recombinant His-tagged enzyme, 90% activity remaining after 120 min Thermochaetoides thermophila
3.2.1.4 70
-
 60 min, enzyme retains 66.2% of its initial activity, xylanase ativity Thermochaetoides thermophila
3.2.1.4 70
-
 60 min, enzyme retains 74.3% of its initial activity, endoglucanase activity Thermochaetoides thermophila
3.2.1.4 70
-
 purified recombinant His-tagged enzyme, 74.3% remaining after 60 min, half-life of endoxylanase activity is 110 min, 30% activity remaining after 120 min Thermochaetoides thermophila
3.2.1.4 80
-
 60 min, enzyme retains 61.3% of its initial activity, endoglucanase activity Thermochaetoides thermophila
3.2.1.4 80
-
 60 min, enzyme retains about 50% of its initial activity, xylanase ativity Thermochaetoides thermophila
3.2.1.4 80
-
 purified recombinant His-tagged enzyme, 61.3% activity remaining after 60 min, half-life of endoxylanase activity is 80 min, 18% activity remaining after 120 min Thermochaetoides thermophila
3.2.1.4 90
-
 40 min, enzyme retains about 28% of its initial activity, endoglucanase activity Thermochaetoides thermophila
3.2.1.4 90
-
 60 min, enzyme retains about 30% of its initial activity, xylanase ativity Thermochaetoides thermophila
3.2.1.4 90
-
 purified recombinant His-tagged enzyme, half-life of endoxylanase activity is 30 min, 20% activity remaining after 60 min, after 120 min Thermochaetoides thermophila
3.2.1.8 60
-
 120 min, enzyme retains about 85% of its initial activity, xylanase ativity Thermochaetoides thermophila
3.2.1.8 60
-
 120 min, enzyme retains more than 80% of its initial activity, endoglucanase activity Thermochaetoides thermophila
3.2.1.8 60
-
 purified recombinant His-tagged enzyme, 90% activity remaining after 120 min Thermochaetoides thermophila
3.2.1.8 70
-
 60 min, enzyme retains 66.2% of its initial activity, xylanase ativity Thermochaetoides thermophila
3.2.1.8 70
-
 60 min, enzyme retains 74.3% of its initial activity, endoglucanase activity Thermochaetoides thermophila
3.2.1.8 70
-
 purified recombinant His-tagged enzyme, half-life of endoxylanase activity is 100 min, 40% activity remaining after 120 min Thermochaetoides thermophila
3.2.1.8 80
-
 60 min, enzyme retains 61.3% of its initial activity, endoglucanase activity Thermochaetoides thermophila
3.2.1.8 80
-
 60 min, enzyme retains about 50% of its initial activity, xylanase ativity Thermochaetoides thermophila
3.2.1.8 80
-
 purified recombinant His-tagged enzyme, half-life of endoxylanase activity is 40 min, 10% activity remaining after 80 min, inactivation after 120 min Thermochaetoides thermophila
3.2.1.8 90
-
 40 min, enzyme retains about 28% of its initial activity, endoglucanase activity Thermochaetoides thermophila
3.2.1.8 90
-
 60 min, enzyme retains about 30% of its initial activity, xylanase ativity Thermochaetoides thermophila
3.2.1.8 90
-
 purified recombinant His-tagged enzyme, half-life of endoxylanase activity is 30 min, inactivation after 80 min Thermochaetoides thermophila

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.4 0.0007
-
 beta-1,4-D-glucan pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.4 0.0007
-
 barley beta-1,4-D-glucan recombinant His-tagged enzyme, pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.4 0.00158
-
 beta-1,4-D-xylan pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.4 0.00211
-
 carboxymethyl cellulose pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.4 0.00211
-
 carboxymethyl cellulose recombinant His-tagged enzyme, pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.8 0.0007
-
 beta-1,4-D-glucan pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.8 0.00158
-
 beta-1,4-D-xylan pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.8 0.00158
-
 beta-1,4-D-xylan recombinant His-tagged enzyme, pH 5.0, 55°C Thermochaetoides thermophila
3.2.1.8 0.00211
-
 carboxymethyl cellulose pH 5.0, 55°C Thermochaetoides thermophila

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.4 5
-
-
 Thermochaetoides thermophila
3.2.1.4 5
-
 for CTendo7's xylanase activity and endoglucanase activity Thermochaetoides thermophila
3.2.1.8 5
-
-
 Thermochaetoides thermophila
3.2.1.8 5
-
 for CTendo7's xylanase activity and endoglucanase activity Thermochaetoides thermophila

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.4 3.5 9.5 activity range, profile overview Thermochaetoides thermophila
3.2.1.4 4 7 pH 4.0: about 75% of maximal activity, pH 7.0: about 35% of maximal activity, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.4 4 7 pH 4.0: about 85% of maximal activity, pH 7.0: about 45% of maximal activity, substrate: xylan Thermochaetoides thermophila
3.2.1.8 3.5 9.5 activity range, profile overview Thermochaetoides thermophila
3.2.1.8 4 7 pH 4.0: about 75% of maximal activity, pH 7.0: about 35% of maximal activity, substrate: carboxymethyl cellulose Thermochaetoides thermophila
3.2.1.8 4 7 pH 4.0: about 85% of maximal activity, pH 7.0: about 45% of maximal activity, substrate: xylan Thermochaetoides thermophila

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.4 Thermochaetoides thermophila sequence calculation
-
 6.02
3.2.1.4 Thermochaetoides thermophila calculated from sequence
-
 6.02
3.2.1.8 Thermochaetoides thermophila sequence calculation
-
 6.02
3.2.1.8 Thermochaetoides thermophila calculated from sequence
-
 6.02

General Information

EC Number General Information Comment Organism
3.2.1.4 additional information the enzyme belongs to the glycosyl hydrolase family 7, GH7. Residue Glu197 acts as the active-site nucleophile and Glu202 is the acid-base catalyst, and this is consistent with a catalytic mechanism leading to a net retention of configuration at the anomeric carbon in the deep substrate binding cleft Thermochaetoides thermophila
3.2.1.8 additional information the enzyme belongs to the glycosyl hydrolase family 7, GH7. Residue Glu197 acts as the active-site nucleophile and Glu202 is the acid-base catalyst, and this is consistent with a catalytic mechanism leading to a net retention of configuration at the anomeric carbon in the deep substrate binding cleft Thermochaetoides thermophila