Urinary levoglucosan levels in Austrian communities differing in agrarian quota

Wallner, Peter; Kundi, Michael; Moshammer, Hanns; Scharf, Sigrid; Schmutzer, M.; Weiß, Stefan; Hohenblum, Philipp; Hutter, Hans-Peter

doi:10.1016/j.ijheh.2012.05.001

International Journal of Hygiene and Environmental Health

2013

DOI: 10.1016/j.ijheh.2012.05.001

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Urinary levoglucosan levels in Austrian communities differing in agrarian quota

Peter Wallner

Michael Kundi

Hanns Moshammer

et al.

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Cited by 9 publications

(1 citation statement)

References 17 publications

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“…LG and other anhydrosugars are also present in soil, thermochemical processing products of biomass, and municipal waste in considerably large amounts (5)(6)(7). Therefore, microbial metabolic pathways of anhydrosugars are recently attracting significant research attention in the context of bioconversion into chemicals and biofuels (8,9).…”

mentioning

confidence: 99%

Identification, functional characterization, and crystal structure determination of bacterial levoglucosan dehydrogenase

Sugiura¹,

Nakahara²,

Yamada

et al. 2018

Journal of Biological Chemistry

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Levoglucosan is the 1,6-anhydrosugar of d-glucose formed by pyrolysis of glucans and is found in the environment and industrial waste. Two types of microbial levoglucosan metabolic pathways are known. Although the eukaryotic pathway involving levoglucosan kinase has been well-studied, the bacterial pathway involving levoglucosan dehydrogenase (LGDH) has not been well-investigated. Here, we identified and cloned the gene from the bacterium and characterized the recombinant protein. The enzyme exhibited high substrate specificity toward levoglucosan and NAD for the oxidative reaction and was confirmed to be LGDH. LGDH also showed weak activities (∼4%) toward l-sorbose and 1,5-anhydro-d-glucitol. The reverse (reductive) reaction using 3-keto-levoglucosan and NADH exhibited significantly lower and higher values than those of the forward reaction. The crystal structures of LGDH in the apo and complex forms with NADH, NADH + levoglucosan, and NADH + l-sorbose revealed that LGDH has a typical fold of Gfo/Idh/MocA family proteins, similar to those of-inositol dehydrogenase, aldose-aldose oxidoreductase, 1,5-anhydro-d-fructose reductase, and glucose-fructose oxidoreductase. The crystal structures also disclosed that the active site of LGDH is distinct from those of these enzymes. The LGDH active site extensively recognized the levoglucosan molecule with six hydrogen bonds, and the C3 atom of levoglucosan was closely located to the C4 atom of NADH nicotinamide. Our study is the first molecular characterization of LGDH, providing evidence for C3-specific oxidation and representing a starting point for future biotechnological use of LGDH and levoglucosan-metabolizing bacteria.

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mentioning

confidence: 99%

Identification, functional characterization, and crystal structure determination of bacterial levoglucosan dehydrogenase

Sugiura¹,

Nakahara²,

Yamada

et al. 2018

Journal of Biological Chemistry

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An overview of particulate emissions from residential biomass combustion

Vicente

Alves

2018

Atmospheric Research

234

116

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Levoglucosan and its hydrolysates via fast pyrolysis of lignocellulose for microbial biofuels: A state-of-the-art review

Jiang

Fang

Zhao

et al. 2019

Renewable and Sustainable Energy Reviews

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Urinary levoglucosan levels in Austrian communities differing in agrarian quota

Cited by 9 publications

References 17 publications

Identification, functional characterization, and crystal structure determination of bacterial levoglucosan dehydrogenase

Identification, functional characterization, and crystal structure determination of bacterial levoglucosan dehydrogenase

An overview of particulate emissions from residential biomass combustion

Levoglucosan and its hydrolysates via fast pyrolysis of lignocellulose for microbial biofuels: A state-of-the-art review

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