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Literature summary extracted from

  • Lee, J.M.; Moon, S.Y.; Kim, Y.R.; Kim, K.W.; Lee, B.J.; Kong, I.S.
    Improvement of thermostability and halostability of endo-1,3-1,4-glucanase by substituting hydrophobic residue for Lys (2017), Int. J. Biol. Macromol., 94, 594-602 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.73 homology modeling of structure. Amino acid residues expected to form hydrogen bond with beta-glucan, nucleophile Glu134, the acid/base catalyst Glu138, Tyr152 and water mediate hydrogen bonds with Asn55, Gln148, Asn150, Glu160, and Asn211, are found in the active site cleft Bacillus sp. SJ-10

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.73 K48A mutation enhances catalytic efficiency, thermostability and halostability Bacillus sp. SJ-10
3.2.1.73 K48L mutation enhances catalytic efficiency, thermostability and halostability Bacillus sp. SJ-10

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.73 additional information
-
Barley beta-glucan Km value of wild-type 2.1 mg/ml, of mutant K48A 1.6 mg/ml, of mutant K48L 1.4 mg/ml, respectively, pH 6.0, 50°C Bacillus sp. SJ-10

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Bacillus sp. SJ-10 I1W007
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 barley beta-glucan + H2O
-
Bacillus sp. SJ-10 ?
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.73 60
-
half-life of wild-type 46.2 min, of mutant K48A 346 min, of mutant K48L 138 min, respectively Bacillus sp. SJ-10
3.2.1.73 70
-
half-life of wild-type 4.5 min, of mutant K48A 30.5 min, of mutant K48L 15.1 min, respectively Bacillus sp. SJ-10

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.73 7.45
-
Barley beta-glucan wild-type, pH 6.0, 50°C Bacillus sp. SJ-10
3.2.1.73 7.45
-
Barley beta-glucan mutant K48A, pH 6.0, 50°C Bacillus sp. SJ-10
3.2.1.73 7.45
-
Barley beta-glucan mutant K48L, pH 6.0, 50°C Bacillus sp. SJ-10

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
-
Barley beta-glucan kcat/Km value of wild-type 3.6 ml/mg/s, of mutant K48A 4.7 ml/mg/s, of mutant K48L 5.2 ml/mg/s, respectively, pH 6.0, 50°C Bacillus sp. SJ-10