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Literature summary extracted from

  • Tyurin, A.; Sadovskaya, N.; Nikiforova, K.; Mustafaev, O.; Komakhin, R.; Fadeev, V.; Goldenkova-Pavlova, I.
    Clostridium thermocellum thermostable lichenase with circular permutations and modifications in the N-terminal region retains its activity and thermostability (2015), Biochim. Biophys. Acta, 1854, 10-19.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.73 expression of wild-type enzyme and mutant circular enzyme constructs in Escherichia coli strain XL1-Blue Acetivibrio thermocellus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.73 additional information construction of hybrid genes encoding circularly permutated lichenase variants with integrated small peptides, i.e. NC-L-53, NC-L-99, NC-L-53-99, and NC-L-140, method overview. Generation of a thermostable lichenase gene variant encoding only the enzyme's catalytic domain LicBM3. Thermostabilities of the mutant constructs, overview Acetivibrio thermocellus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.73 Acetivibrio thermocellus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 lichenan + H2O
-
 Acetivibrio thermocellus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.73 endo-beta-1,3;1,4-glucan-D-glycosyl hydrolase
-
 Acetivibrio thermocellus
3.2.1.73 Lichenase
-
 Acetivibrio thermocellus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.73 70
-
 assay at Acetivibrio thermocellus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.73 8
-
 assay at Acetivibrio thermocellus

General Information

EC Number General Information Comment Organism
3.2.1.73 additional information in silico analysis and structure homology modelling of the enzyme's catalytic domain, LicBM3, secondary structure Acetivibrio thermocellus