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Literature summary for 3.2.1.4 extracted from

  • Wang, Y.; Yuan, H.; Wang, J.; Yu, Z.
    Truncation of the cellulose binding domain improved thermal stability of endo-beta-1,4-glucanase from Bacillus subtilis JA18 (2009), Biores. Technol., 100, 345-349.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
additional information C-terminus truncation mutant Egl330, truncation of the cellulose binding domain, a great improvement in thermal stability is observed in Egl330 Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
carboxymethylcellulose binding of the cellulose-binding domain to avicel is inhibited by carboxymethylcellulose, but not by barley beta-glucan and glucose at concentration of 0.1% and 0.5% Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
carboxymethylcellulose Km of Egl330 and Egl499 are 1.73 x 10 mg/ml and 1.14 x 10 mg/ml, respectively. Vmax of Egl330 is 1.78fold higher than that of Egl499, increases from 284 U/mg to 786 U/mg. The catalytic efficiency (kcat/Km) of Egl330 is slightly higher than that of Egl499 Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31000
-
C-terminus truncation mutant Egl330, calculated Bacillus subtilis
36000
-
C-terminus truncation mutant Egl330, calculated Bacillus subtilis
50000
-
Egl499 wild-type, SDS-PAGE Bacillus subtilis
55000
-
Egl499 wild-type, SDS-PAGE Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
JA18
-
Bacillus subtilis JA18
-
JA18
-

Purification (Commentary)

Purification (Comment) Organism
affinity chromatography on Ni-NTA column Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
barley beta-glucan + H2O soluble substrate Bacillus subtilis ?
-
?
barley beta-glucan + H2O soluble substrate Bacillus subtilis JA18 ?
-
?
carboxymethylcellulose + H2O soluble substrate Bacillus subtilis ?
-
?
carboxymethylcellulose + H2O soluble substrate Bacillus subtilis JA18 ?
-
?
cellulose + H2O
-
Bacillus subtilis ?
-
?
cellulose + H2O
-
Bacillus subtilis JA18 ?
-
?
additional information wild-type and mutant can not hydrolyze Avicel, laminarin and chitosan Bacillus subtilis ?
-
?
additional information wild-type and mutant can not hydrolyze Avicel, laminarin and chitosan Bacillus subtilis JA18 ?
-
?

Synonyms

Synonyms Comment Organism
Egl499
-
Bacillus subtilis
endo-beta-1,4-glucanase
-
Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
assay at Bacillus subtilis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 75 optimal enzymatic reaction temperature tested Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65 80
-
Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis shows both the turnover rate (kcat) and the catalytic efficiency (kcat/Km) of Egl330 increased for the substrate carboxymethylcellulose compared to Egl499 Bacillus subtilis
246
-
carboxymethylcellulose wild-type Bacillus subtilis
437
-
carboxymethylcellulose the turnover rate (kcat) of Egl330 increased by 78% compared to wild-type Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.8
-
assay at Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
4.5 7
-
Bacillus subtilis