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Literature summary for 3.2.1.73 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
Search for more literature for 3.2.1.73

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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

Organism UniProt Comment Textmining
Acetivibrio thermocellus
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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