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Literature summary for 1.14.99.54 extracted from

  • Arfi, Y.; Shamshoum, M.; Rogachev, I.; Peleg, Y.; Bayer, E.A.
    Integration of bacterial lytic polysaccharide monooxygenases into designer cellulosomes promotes enhanced cellulose degradation (2014), Proc. Natl. Acad. Sci. USA, 111, 9109-9114.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
degradation design of dockerin-fused lytic polysaccharide monooxygenases. The resulting chimeras exhibit activity levels on microcrystalline cellulose similar to that of the wild-type enzymes. The dockerin moieties of the chimeras are functional and specifically bind to their corresponding cohesin partner. The chimeric lytic polysaccharide monooxygenases are able to self-assemble in designer cellulosomes alongside an endo- and an exo-cellulase also converted to the cellulosomal mode. The resulting complexes show a 1.7fold increase in the release of soluble sugars from cellulose, compared with the free enzymes, and a 2.6fold enhancement compared with free cellulases without lytic polysaccharide monooxygenase enhancement Thermobifida fusca

Organism

Organism UniProt Comment Textmining
Thermobifida fusca Q47PB9
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Thermobifida fusca Q47QG3 enzyme has both C1-hydroxylating and C4-dehydrogenating activities
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
microcrystalline cellulose + AH2 + O2
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Thermobifida fusca ? enzyme catalyzes release of a mixture of soluble sugars comprising reduced and oxidized cellooligosaccharides. The degree of polymerization of the released oligosaccharides ranges from 3 to 5 for the reduced products and from 2 to 5 for the oxidized products ?

Synonyms

Synonyms Comment Organism
LPMO10A
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Thermobifida fusca
LPMO10B
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Thermobifida fusca
Tfu_1268
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Thermobifida fusca
Tfu_1665
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Thermobifida fusca