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1 egrading enzymes from cellulolytic bacterium Thermobifida fusca , we show that the model can be used
2 -glucosidase from the thermophilic bacterium Thermobifida fusca and inserted into the tobacco (Nicoti
3 activities of nine thermal stable mutants of Thermobifida fusca BglC were assayed by isothermal titra
4 nd between an inactive endocellulase mutant (Thermobifida fusca Cel6A D117Acd) and four oligosacchari
6 nserved noncatalytic active site residues of Thermobifida fusca Cel6B were constructed, cloned and ex
8 ribing the steady-state binding of MUS-CB to Thermobifida fusca cellulase Cel6A are similar to those
9 bility of a high-resolution structure of the Thermobifida fusca endocellulase Cel6A catalytic domain
11 lulase, Cel48A, formerly E6, was cloned from Thermobifida fusca into Escherichia coli and Streptomyce
15 ases in the cellulose-degrading actinomycete Thermobifida fusca is controlled by a transcriptional re
17 nced genome of the thermophilic actinomycete Thermobifida fusca revealed an orphan nonribosomal pepti
19 acterized laccase from the aerobic bacterium Thermobifida fusca The resultant chimera exhibited activ
20 Here we present two cryo-EM snapshots of the Thermobifida fusca type I-E Cascade: (1) unwinding 11 bp
23 6, Nocardioides sp. strain JS614 TOPRIM, and Thermobifida fusca YX Tfu2914 inteins have a mixture of
24 e cellulolytic enzymes in the model organism Thermobifida fusca, but only Nocardiopsis dassonvillei s
25 and characterizing evolution experiments on Thermobifida fusca, we were able to show that evolutiona
26 strains of the cellulolytic actinobacterium, Thermobifida fusca, were generated for two different sce
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