The chitinolytic machinery of Serratia marcescens – a model system for enzymatic degradation of recalcitrant polysaccharides
TLDR
The catalytic mechanisms of these enzymes as well as the structural basis of each enzyme's specific role in the chitin degradation process are discussed, and how knowledge of this enzyme system may be extrapolated to other enzyme systems for conversion of insoluble polysaccharides is discussed.Abstract:
The chitinolytic machinery of Serratia marcescens is one of the best known enzyme systems for the conversion of insoluble polysaccharides This machinery includes four chitin-active enzymes: ChiC, an endo-acting non-processive chitinase; ChiA and ChiB, two processive chitinases moving along chitin chains in opposite directions; and CBP21, a surface-active CBM33-type lytic polysaccharide monooxygenase that introduces chain breaks by oxidative cleavage Furthermore, an N-acetylhexosaminidase or chitobiase converts the oligomeric products from the other enzymes to monomeric N-acetylglucosamine Here we discuss the catalytic mechanisms of these enzymes as well as the structural basis of each enzyme's specific role in the chitin degradation process We also discuss how knowledge of this enzyme system may be extrapolated to other enzyme systems for conversion of insoluble polysaccharides, in particular conversion of cellulose by cellulases and GH61-type lytic polysaccharide monooxygenasesread more
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Chemical and biological catalysis for plastics recycling and upcycling
Lucas D. Ellis,Nicholas A. Rorrer,Kevin P. Sullivan,Maike Otto,John McGeehan,Yuriy Román-Leshkov,Nick Wierckx,Gregg T. Beckham +7 more
TL;DR: In this article, the challenges and opportunities associated with the catalytic transformation of waste plastics, looking at both chemical and biological approaches to transforming such spent materials into a resource, are explored and compared.
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Lytic Polysaccharide Monooxygenases in Biomass Conversion
TL;DR: LPMOs offer tremendous promise for further process improvements owing to their ability to boost the activity of biomass-degrading enzyme consortia, and the academic literature in this area is reviewed.
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Recent insights into copper-containing lytic polysaccharide mono-oxygenases.
TL;DR: 3D structural analyses of lytic polysaccharide mono-oxygenases of both bacterial and fungal enzymes revealed structures with β-sandwich folds containing an active site with a metal coordinated by an N-terminal histidine, indicating copper-dependent oxygenases.
Journal ArticleDOI
The Copper Active Site of Cbm33 Polysaccharide Oxygenases.
Glyn R. Hemsworth,Edward J. Taylor,Robbert Q. Kim,Rebecca C. Gregory,Sally J. Lewis,Johan P. Turkenburg,Alison Parkin,Gideon J. Davies,Paul H. Walton +8 more
TL;DR: The capacity of metal-dependent fungal and bacterial polysaccharide oxygenases, termed GH61 and CBM33, respectively, to potentiate the enzymatic degradation of cellulose opens new possibilities for the conversion of recalcitrant biomass to bio fuels.
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A rapid quantitative activity assay shows that the Vibrio cholerae colonization factor GbpA is an active lytic polysaccharide monooxygenase.
Jennifer S. M. Loose,Zarah Forsberg,Marco W. Fraaije,Vincent G. H. Eijsink,Gustav Vaaje-Kolstad +4 more
TL;DR: A method for quantification of C1‐oxidized chitooligosaccharides (aldonic acids) and hence LPMO activity is described, used to quantify the activity of a four‐domain L PMO from Vibrio cholerae, GbpA, which is a virulence factor with no obvious role in biomass processing.
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