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Literature summary extracted from

  • Gargallo, R.; Cedano, J.; Mozo-Villarias, A.; Querol, E.; Oliva, B.
    Study of the influence of temperature on the dynamics of the catalytic cleft in 1,3-1,4-beta-glucanase by molecular dynamics simulations (2006), J. Mol. Model., 12, 835-845.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.6 N207D increase in Tm-value to 75.3°C, compared to wild-type Tm-value of 71.4°C Bacillus licheniformis
3.2.1.73 N207D mutant displays better thermotolerance than the wild type but also reduced activity Bacillus licheniformis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.73 Ca2+ necessary for the activity of the enzyme Bacillus licheniformis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.6 Bacillus licheniformis
-
-
-
3.2.1.73 Bacillus licheniformis P27051
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucopyranoside + H2O
-
Bacillus licheniformis 4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucopyranoside
-
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Synonyms

EC Number Synonyms Comment Organism
3.2.1.73 1,3-1,4-beta-glucanase
-
Bacillus licheniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.6 additional information
-
hypothesis for thermal inactivation: the first phase in thermal denaturation could be produced when calcium interactions are disrupted and the main loop becomes free to rearrange. This phase yields a partially active intermediary during the first phase of inactivation and then the intermediary is slowly converted into a totally inactive enzyme in the second phase Bacillus licheniformis
3.2.1.6 71
-
Tm-value for wild-type enzyme is 71.4°C Bacillus licheniformis
3.2.1.6 75
-
Tm-value for mutant enzyme N207D is 75.3°C Bacillus licheniformis