Identification of an extracellular bacterial flavoenzyme that can prevent re-polymerisation of lignin fragments.
A significant problem in the oxidative breakdown of lignin is the tendency of phenolic radical fragments to re-polymerise to form higher molecular weight species. In this paper we identify an extracellular flavin-dependent dehydrolipoamide dehydrogenase from Thermobifida fusca that prevents oxidative dimerization of a dimeric lignin model compound, which could be used as an accessory enzyme for lignin depolymerisation.
Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK.
Rahman
R
Rahmanpour
Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK.
Lloyd D W
LD
King
Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK. Electronic address: T.D.Bugg@warwick.ac.uk.
Timothy D H
TD
Bugg
D039903:Actinobacteria / Q000201:enzymology*; D008058:Dihydrolipoamide Dehydrogenase / Q000378:metabolism*; D045604:Extracellular Fluid / Q000378:metabolism*; D005420:Flavoproteins / Q000378:metabolism; D008031:Lignin / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D055503:Protein Multimerization
D005420:Flavoproteins; D010446:Peptide Fragments; D008031:Lignin; D008058:Dihydrolipoamide Dehydrogenase
Dihydrolipoamide dehydrogenase; Lignin degradation; Thermobifida fusca