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Literature summary extracted from

  • Andre, G.; Kanchanawong, P.; Palma, R.; Cho, H.; Deng, X.; Irwin, D.; Himmel, M.E.; Wilson, D.B.; Brady, J.W.
    Computational and experimental studies of the catalytic mechanism of Thermobifida fusca cellulase Cel6A (E2) (2003), Protein Eng., 16, 125-134.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.4 R78A activity with phosphoric acid-swollen cellulose is less than 1.3% of the wild-type activity, activity with carboxymethylcellulose is less than 0.9% of the wild-type activity, activity with bacterial microcrystalline cellulose is less than 18.7% of the wild-type activity Thermobifida fusca
3.2.1.4 R78K activity with phosphoric acid-swollen cellulose is 54% of the wild-type activity, activity with carboxymethylcellulose is 15% of the wild-type activity, activity with bacterial microcrystalline cellulose is 52% of the activity with wild-type enzyme Thermobifida fusca

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.4 Thermobifida fusca
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.4 bacterial micropcrystalline cellulose + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.4 carboxymethylcellulose + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.4 additional information Arg78 participates in catalysis Thermobifida fusca ?
-
 ?
3.2.1.4 phosphoric acid-swollen cellulose + H2O
-
 Thermobifida fusca ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.4 Cel6A (E2)
-
 Thermobifida fusca