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Classification of fungal and bacterial lytic polysaccharide monooxygenases

Overview of attention for article published in BMC Genomics, May 2015
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Classification of fungal and bacterial lytic polysaccharide monooxygenases
Published in
BMC Genomics, May 2015
DOI 10.1186/s12864-015-1601-6
Pubmed ID

Peter K Busk, Lene Lange


Lytic polysaccharide monooxygenases are important enzymes for the decomposition of recalcitrant biological macromolecules such as plant cell wall and chitin polymers. These enzymes were originally designated glycoside hydrolase family 61 and carbohydrate-binding module family 33 but are now classified as auxiliary activities 9, 10 and 11 in the CAZy database. To obtain a systematic analysis of the divergent families of lytic polysaccharide monooxygenases we used Peptide Pattern Recognition to divide 5396 protein sequences resembling enzymes from families AA9 (1828 proteins), AA10 (2799 proteins) and AA11 (769 proteins) into subfamilies. The results showed that the lytic polysaccharide monooxygenases have two conserved regions identified by conserved peptides specific for each AA family. The peptides were used for in silico PCR discovery of the lytic polysaccharide monooxygenases in 79 fungal and 95 bacterial genomes. The bacterial genomes encoded 0 - 7 AA10s (average 0.6). No AA9 or AA11 were found in the bacteria. The fungal genomes encoded 0 - 40 AA9s (average 7) and 0 - 15 AA11s (average 2) and two of the fungi possessed a gene encoding a putative AA10. The AA9s were mainly found in plant cell wall-degrading asco- and basidiomycetes in agreement with the described role of AA9 enzymes. In contrast, the AA11 proteins were found in 36 of the 39 ascomycetes and in only two of the 32 basidiomycetes and their abundance did not correlate to the degradation of cellulose and hemicellulose. These results provides an overview of the sequence characteristics and occurrence of the divergent AA9, AA10 and AA11 families and pave the way for systematic investigations of the of lytic polysaccharide monooxygenases and for structure-function studies of these enzymes.

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Mendeley readers

The data shown below were compiled from readership statistics for 178 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Colombia 1 <1%
Switzerland 1 <1%
France 1 <1%
Italy 1 <1%
Austria 1 <1%
Australia 1 <1%
Sweden 1 <1%
Finland 1 <1%
Unknown 170 96%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 43 24%
Researcher 43 24%
Student > Master 26 15%
Student > Bachelor 17 10%
Student > Doctoral Student 7 4%
Other 25 14%
Unknown 17 10%
Readers by discipline Count As %
Agricultural and Biological Sciences 66 37%
Biochemistry, Genetics and Molecular Biology 55 31%
Chemistry 13 7%
Environmental Science 4 2%
Engineering 3 2%
Other 10 6%
Unknown 27 15%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 13 May 2015.
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