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Literature summary extracted from

  • Sun, J.; Wang, H.; Lv, W.; Ma, C.; Lou, Z.; Dai, Y.
    Construction and characterization of a fusion beta-1,3-1,4-glucanase to improve hydrolytic activity and thermostability (2011), Biotechnol. Lett., 33, 2193-2199.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.73 synthesis construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30% Bacillus amyloliquefaciens
3.2.1.73 synthesis construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30% Acetivibrio thermocellus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.73 expression in Escherichia coli Bacillus amyloliquefaciens
3.2.1.73 expression in Escherichia coli Acetivibrio thermocellus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.73 additional information construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30% Bacillus amyloliquefaciens
3.2.1.73 additional information construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80°C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30% Acetivibrio thermocellus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.73 additional information
-
 additional information KM value for native enzyme, substrate beta-D-glucan, is 1.5 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1.2 mg/ml Bacillus amyloliquefaciens
3.2.1.73 additional information
-
 additional information KM value for native enzyme, substrate beta-D-glucan, is 2.7 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1.2 mg/ml Acetivibrio thermocellus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Acetivibrio thermocellus Q84C00
-
-
3.2.1.73 Bacillus amyloliquefaciens Q84F88
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.73 192
-
 native enzyme, substrate lichenan, pH 6.0, 70°C Acetivibrio thermocellus
3.2.1.73 275
-
 native enzyme, substrate beta-D-glucan, pH 6.0, 70°C Acetivibrio thermocellus
3.2.1.73 851
-
 native enzyme, substrate lichenan, pH 6.0, 50°C Bacillus amyloliquefaciens
3.2.1.73 1106
-
 native enzyme, substrate beta-D-glucan, pH 6.0, 50°C Bacillus amyloliquefaciens
3.2.1.73 1746
-
 fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70°C Bacillus amyloliquefaciens
3.2.1.73 1746
-
 fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70°C Acetivibrio thermocellus
3.2.1.73 2434
-
 fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70°C Bacillus amyloliquefaciens
3.2.1.73 2434
-
 fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70°C Acetivibrio thermocellus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 beta-D-glucan + H2O source of substrate: oat Bacillus amyloliquefaciens ?
-
 ?
3.2.1.73 beta-D-glucan + H2O source of substrate: oat Acetivibrio thermocellus ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Bacillus amyloliquefaciens ?
-
 ?
3.2.1.73 lichenan + H2O
-
 Acetivibrio thermocellus ?
-
 ?
3.2.1.73 additional information no substrate: carboxymethyl cellulose, xylan from birch, soluble starch Bacillus amyloliquefaciens ?
-
 ?
3.2.1.73 additional information no substrate: carboxymethyl cellulose, xylan from birch, soluble starch Acetivibrio thermocellus ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.73 2.3
-
 Beta-D-glucan native enzyme, pH 6.0, 70°C Acetivibrio thermocellus
3.2.1.73 9.2
-
 Beta-D-glucan native enzyme, pH 6.0, 50°C Bacillus amyloliquefaciens
3.2.1.73 20.3
-
 Beta-D-glucan fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70°C Bacillus amyloliquefaciens
3.2.1.73 20.3
-
 Beta-D-glucan fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70°C Acetivibrio thermocellus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.73 additional information
-
 additional information Kcat/KM value for native enzyme, substrate beta-D-glucan, is 369 mg/ml/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1014 mg/ml/min Bacillus amyloliquefaciens
3.2.1.73 additional information
-
 additional information kcat/KM value for native enzyme, substrate beta-D-glucan, is 51 ml/mg/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1014 ml/mg/min Acetivibrio thermocellus