- Title
- Bioinformatic characterization of type-specific sequence and structural features in auxiliary activity family 9 proteins:
- Creator
- Moses, Vuyani
- Creator
- Hatherley, Rowan
- Creator
- Tastan Bishop, Özlem
- Date Issued
- 2016
- Date
- 2016
- Type
- text
- Type
- article
- Identifier
- http://hdl.handle.net/10962/148358
- Identifier
- vital:38732
- Identifier
- DOI: 10.1186/s13068-016-0655-2
- Description
- Due to the impending depletion of fossil fuels, it has become important to identify alternative energy sources. The biofuel industry has proven to be a promising alternative. However, owing to the complex nature of plant biomass, hence the degradation, biofuel production remains a challenge. The copper-dependent Auxiliary Activity family 9 (AA9) proteins have been found to act synergistically with other cellulose-degrading enzymes resulting in an increased rate of cellulose breakdown. AA9 proteins are lytic polysaccharide monooxygenase (LPMO) enzymes, otherwise known as polysaccharide monooxygenases (PMOs). They are further classified as Type 1, 2 or 3 PMOs, depending on the different cleavage products formed. As AA9 proteins are known to exhibit low sequence conservation, the analysis of unique features of AA9 domains of these enzymes should provide insights for the better understanding of how different AA9 PMO types function.
- Format
- Language
- English
- Relation
- Biotechnology for biofuels
- Relation
- Moses, V., Hatherley, R. and Bishop, Ö.T., 2016. Bioinformatic characterization of type-specific sequence and structural features in auxiliary activity family 9 proteins. Biotechnology for biofuels, 9(1), p.239.
- Relation
- Biotechnology for biofuels volume 9 number 1 p.239 2016 1754-6834
- Rights
- Publisher
- Rights
- Use of this resource is governed by the terms and conditions of the BioMed Central Limited Terms and Conditions statement (https://www.biomedcentral.com/terms-and-conditions)
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