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Literature summary for 3.2.1.91 extracted from

  • Kataeva, I.A.; Brewer, J.M.; Uversky, V.N.; Ljungdahl, L.G.
    Domain coupling in a multimodular cellobiohydrolase CbhA from Clostridium thermocellum (2005), FEBS Lett., 579, 4367-4373.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain BL21(DE3) of the enzyme domain constructs: X1 2, X1 1/X1 2, CBD3, X1 1/X1 2-CBD3, Ig, GH9, Ig-GH9, Ig-GH9-X1 1/X1 2, and Ig-GH9-X1 1/X1 2-CBD3, overview Acetivibrio thermocellus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ bound by all enzyme domains, except for the immunoglobulin-like module Acetivibrio thermocellus

Organism

Organism UniProt Comment Textmining
Acetivibrio thermocellus Q59325 gene cbhA
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Acetivibrio thermocellus JW20 Q59325 gene cbhA
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme domain constructs from Escherichia coli strain BL21(DE3) to near homogeneity by nickel affinity chromatography and gel filtration Acetivibrio thermocellus

Subunits

Subunits Comment Organism
More the enzyme is composed of an N-terminal carbohydrate-binding module of family 4 CBD4, an immunoglobulin-like module Ig, a catalytic module of glycoside hydrolase family 9 GH9, X1 1 and X1 2 modules, a carbohydrate-binding module of family 3 CBD3, and finally a C-terminal dockerin module, intramolecular interaction analysis, residues T230, D262, and D264 are important, analysis of doamin coupling, overview Acetivibrio thermocellus

Synonyms

Synonyms Comment Organism
CbhA
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Acetivibrio thermocellus
cellobiohydrolase A
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Acetivibrio thermocellus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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irreversible thermal unfolding kinetics of recombinant enzyme domains, overview Acetivibrio thermocellus