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1 an EGase catalytic domain from the bacterium Thermobifida fusca.
2 ed LPMOs based on enzymes from the bacterium Thermobifida fusca.
3 3A) from the aerobic cellulolytic bacterium, Thermobifida fusca.
4 -glucosidase from the thermophilic bacterium Thermobifida fusca and inserted into the tobacco (Nicoti
5 activities of nine thermal stable mutants of Thermobifida fusca BglC were assayed by isothermal titra
6 e cellulolytic enzymes in the model organism Thermobifida fusca, but only Nocardiopsis dassonvillei s
7 nd between an inactive endocellulase mutant (Thermobifida fusca Cel6A D117Acd) and four oligosacchari
9 nserved noncatalytic active site residues of Thermobifida fusca Cel6B were constructed, cloned and ex
11 ribing the steady-state binding of MUS-CB to Thermobifida fusca cellulase Cel6A are similar to those
12 e genome of the thermophilic actinobacterium Thermobifida fusca encodes for a lasso peptide with an u
13 bility of a high-resolution structure of the Thermobifida fusca endocellulase Cel6A catalytic domain
15 lulase, Cel48A, formerly E6, was cloned from Thermobifida fusca into Escherichia coli and Streptomyce
19 ases in the cellulose-degrading actinomycete Thermobifida fusca is controlled by a transcriptional re
21 nced genome of the thermophilic actinomycete Thermobifida fusca revealed an orphan nonribosomal pepti
24 acterized laccase from the aerobic bacterium Thermobifida fusca The resultant chimera exhibited activ
25 Here we present two cryo-EM snapshots of the Thermobifida fusca type I-E Cascade: (1) unwinding 11 bp
27 egrading enzymes from cellulolytic bacterium Thermobifida fusca , we show that the model can be used
28 and characterizing evolution experiments on Thermobifida fusca, we were able to show that evolutiona
29 strains of the cellulolytic actinobacterium, Thermobifida fusca, were generated for two different sce
31 6, Nocardioides sp. strain JS614 TOPRIM, and Thermobifida fusca YX Tfu2914 inteins have a mixture of