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Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose...

Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_slubar_slu_se_79374

Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase

About this item

Full title

Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2016-05, Vol.113 (21), p.5922-5927

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze oxidative cleavage of glycosidic bonds using molecular oxygen and an external electron donor. We have used NMR and isothermal titration calorimetry (ITC) to study the interactions of a broad-specificity fungal LPMO, NcLPMO9C, with various substrates and with cell...

Alternative Titles

Full title

Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_swepub_primary_oai_slubar_slu_se_79374

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_slubar_slu_se_79374

Other Identifiers

ISSN

0027-8424,1091-6490

E-ISSN

1091-6490

DOI

10.1073/pnas.1602566113

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