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Literature summary extracted from

  • Vuong, T.V.; Wilson, D.B.
    Processivity, synergism, and substrate specificity of Thermobifida fusca Cel6B (2009), Appl. Environ. Microbiol., 75, 6655-6661.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.91 cloning in Escherichia coli strain DH5alpha, expression of wild-type and mutant enzymes in Escherichia coli strain BL21 RPIL DE3 Thermobifida fusca

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.91 D512A site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme Thermobifida fusca
3.2.1.91 L230A site-directed mutagenesis, the mutation causes slightly increased processivity and increased activity with phosphoric acid-treated cotton over 250%, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme Thermobifida fusca
3.2.1.91 M514A site-directed mutagenesis, the mutation alters the secondary structure of the enzyme, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme Thermobifida fusca
3.2.1.91 M514Q site-directed mutagenesis, the mutation alters the secondary structure of the enzyme, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme Thermobifida fusca
3.2.1.91 additional information mixtures of the Cel6B mutant enzymes and Thermobifida fusca endocellulase Cel5A do not show increased synergism or processivity, and the mutant enzyme which has the highest processivity give the poorest synergism Thermobifida fusca
3.2.1.91 N282A site-directed mutagenesis, mutation in residue near the tunnel entrance causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme Thermobifida fusca
3.2.1.91 N282D site-directed mutagenesis, mutation in residue near the tunnel entrance causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme Thermobifida fusca
3.2.1.91 R180A site-directed mutagenesis, mutation in residue near the tunnel exit causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme Thermobifida fusca
3.2.1.91 R180K site-directed mutagenesis, mutation in residue near the tunnel exit causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme Thermobifida fusca
3.2.1.91 W464A site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme Thermobifida fusca
3.2.1.91 W464Y site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme Thermobifida fusca

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.91 cellulose + H2O Thermobifida fusca cellobiohydrolases act from one end of a cellulose chain and processively cleave off cellobiose as the main product. Processivity and synergism are important properties of cellulases, particularly for hydrolysis of crystalline substrates ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.91 Thermobifida fusca
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.91 cellulose + H2O cellobiohydrolases act from one end of a cellulose chain and processively cleave off cellobiose as the main product. Processivity and synergism are important properties of cellulases, particularly for hydrolysis of crystalline substrates Thermobifida fusca ?
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 ?
3.2.1.91 cellulose + H2O substrates are phosphoric acid-treated cotton, carboxymethylcellulose, bacterial microcrystalline cellulose, and phosphoric acid-swollen cellulose, as well as 8-mg/ml Whatman no. 1 filter paper, substrate specificity of wild-type and mutant enzymes, overview Thermobifida fusca ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.91 Cel6B
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 Thermobifida fusca
3.2.1.91 cellobiohydrolase
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 Thermobifida fusca
3.2.1.91 exocellulase
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 Thermobifida fusca

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.91 50
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 assay at Thermobifida fusca

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.91 5.5
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 assay at Thermobifida fusca