Isolation of the (+)-Pinoresinol-Mineralizing Pseudomonas sp. Strain SG-MS2 and Elucidation of Its Catabolic Pathway

@article{Shettigar2017IsolationOT,
  title={Isolation of the (+)-Pinoresinol-Mineralizing Pseudomonas sp. Strain SG-MS2 and Elucidation of Its Catabolic Pathway},
  author={Madhura Shettigar and Sahil Balotra and David M. Cahill and Andrew C. Warden and Michael James Lacey and Hans-Peter E. Kohler and Daniel Rentsch and John G. Oakeshott and Gunjan Pandey},
  journal={Applied and Environmental Microbiology},
  year={2017},
  volume={84}
}
ABSTRACT Pinoresinol is a dimer of two β-β′-linked coniferyl alcohol molecules. It is both a plant defense molecule synthesized through the shikimic acid pathway and a representative of several β-β-linked dimers produced during the microbial degradation of lignin in dead plant material. Until now, little has been known about the bacterial catabolism of such dimers. Here we report the isolation of the efficient (+)-pinoresinol-mineralizing Pseudomonas sp. strain SG-MS2 and its catabolic pathway… 
7 Citations
Oxidative Catabolism of (+)-Pinoresinol Is Initiated by an Unusual Flavocytochrome Encoded by Translationally Coupled Genes within a Cluster of (+)-Pinoresinol-Coinduced Genes in Pseudomonas sp. Strain SG-MS2
TLDR
Comp comparative genomics, proteomics, protein semipurification, and heterologous expression are used to identify a flavoprotein from the vanillyl alcohol oxidase/p-cresol methyl hydroxylase (VAO/PCMH) enzyme family in SG-MS2 that carries out the initial hydroxymation of (+)-pinoresinol at the benzylic carbon.
The Hydroxyquinol Degradation Pathway in Rhodococcus jostii RHA1 and Agrobacterium Species Is an Alternative Pathway for Degradation of Protocatechuic Acid and Lignin Fragments
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This study has found the existence of a second pathway for degradation of protocatechuic acid in Rhodococcus jostii RHA1, via hydroxyquinol (benzene-1,2,4-triol), which establishes a metabolic link between protocatechuate 3, 4-dioxygenase and hydroxychinol.
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The P. fluorescens decarboxylase enzyme showed enhanced carboligase activity between vanillin and acetaldehyde, rationalized by the presence of alanine versus serine at residue 73 in the enzyme active site, which was investigated further by site-directed mutagenesis of this residue.
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The eLignin database is introduced, its dataset is used to map the reported ecological and biochemical diversity of the lignin microbial niches, and the findings are discussed.
Vanillyl alcohol oxidase.
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This review presents a historical outline of the research on vanillyl alcohol oxidase (VAO) from Penicillium simplicissimum, one of the canonical members of the VAO/PCMH flavoprotein family, and discusses the physiological role, substrate scope, and catalytic mechanism of VAO.
Advances in microbial lignin degradation and its applications.
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This review focuses on microbial enzymes that are responsible for lignin degradation and on their applications to biological lignocellulosic biomass pretreatment and biotechnological lign in engineering.
Potential use of bacteria collected from human hands for textile dye decolorization
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