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Literature summary extracted from

  • Li, Y.; Wilson, D.B.
    Chitin binding by Thermobifida fusca cellulase catalytic domains (2008), Biotechnol. Bioeng., 100, 644-652.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.4 expressed in Streptomyces lividans TKM31 and Escherichia coli BL21 Thermobifida fusca

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.4 D261A/R378K Cel9A mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center. Mutant has weak chitinase activity, but no soluble products are detected Thermobifida fusca
3.2.1.4 G234S Cel6B mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center Thermobifida fusca
3.2.1.4 W329C Cel6B mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center Thermobifida fusca
3.2.1.4 W332A Cel6B mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center Thermobifida fusca
3.2.1.4 Y206F Cel9A mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center Thermobifida fusca
3.2.1.4 Y206S Cel9A mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center Thermobifida fusca

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.4 phenyl-Sepharose column, followed by a Q-Sepharose column, assessed by SDS-PAGE Thermobifida fusca

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.4 4-methylumbelliferyl beta-cellotrioside + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.4 alpha-chitin + H2O due to the binding, it seems chitin would be an inhibitor of Cel6B, Cel9A and Cel48A, but not of Cel6A and Cel5A Thermobifida fusca ?
-
 ?
3.2.1.4 cellobiose + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.4 cellotetraose + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.4 cellotriose + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.4 cellulose + H2O the catalytic domains of Cel6A, Cel6B, Cel48A, Cel5A, and Cel9A only show very weak binding to bacterial cellulose Thermobifida fusca ?
-
 ?
3.2.1.4 chitotetraose + H2O
-
 Thermobifida fusca ?
-
 ?
3.2.1.4 chitotriose + H2O
-
 Thermobifida fusca ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.4 Cellulase
-
 Thermobifida fusca
3.2.1.4 endocellulase
-
 Thermobifida fusca

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.4 50
-
 assay at Thermobifida fusca

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.4 5.5
-
 assay at Thermobifida fusca