Characterization of<i>ligV</i>Essential for Catabolism of Vanillin by<i>Sphingomonas paucimobilis</i>SYK-6

Masai, Eiji; Yamamoto, Yuko; Inoue, Tatsuro; Takamura, Kazuhiro; Hara, Hirofumi; Kasai, Daisuke; Katayama, Yoshihiro; Fukuda, Masao

doi:10.1271/bbb.70267

Cited by 60 publications

(48 citation statements)

References 23 publications

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“…Even though LigV showed a broad range of activity against benzaldehyde derivatives, the activity for SN was considerably lower than that for VN. Further, disruption of ligV minimally affected the growth of SYK-6 on SN25. These results suggest that an alternative aromatic ALDH gene is involved in the catabolism of SN in SYK-6.…”

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confidence: 74%

“…The substrate range of some VN dehydrogenases for benzaldehyde derivatives, including SN, has been determined242526; however, these aromatic dehydrogenases have weak SN oxidation activity. These findings imply the presence of other aromatic aldehyde dehydrogenase (ALDH) genes that are responsible for the oxidation of SN.…”

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confidence: 99%

“…Over 30 genes of SYK-6 responsible for the upper funneling pathway and lower ring-cleavage pathways have been identified and characterized5. Among these genes, the VN dehydrogenase gene ( ligV ), which is essential for the catabolism of VN, was isolated by shotgun cloning25. The deduced amino acid sequence of ligV exhibited 35–53% identity with those of the known VN dehydrogenase genes of Pseudomonas 21, Rhodococcus 27, Corynebacterium 24, and Amycolatopsis 18.…”

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confidence: 99%

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A bacterial aromatic aldehyde dehydrogenase critical for the efficient catabolism of syringaldehyde

Kamimura

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Takahashi

et al. 2017

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Vanillin and syringaldehyde obtained from lignin are essential intermediates for the production of basic chemicals using microbial cell factories. However, in contrast to vanillin, the microbial conversion of syringaldehyde is poorly understood. Here, we identified an aromatic aldehyde dehydrogenase (ALDH) gene responsible for syringaldehyde catabolism from 20 putative ALDH genes of Sphingobium sp. strain SYK-6. All these genes were expressed in Escherichia coli, and nine gene products, including previously characterized BzaA, BzaB, and vanillin dehydrogenase (LigV), exhibited oxidation activities for syringaldehyde to produce syringate. Among these genes, SLG_28320 (desV) and ligV were most highly and constitutively transcribed in the SYK-6 cells. Disruption of desV in SYK-6 resulted in a significant reduction in growth on syringaldehyde and in syringaldehyde oxidation activity. Furthermore, a desV ligV double mutant almost completely lost its ability to grow on syringaldehyde. Purified DesV showed similar kcat/Km values for syringaldehyde (2100 s−1·mM−1) and vanillin (1700 s−1·mM−1), whereas LigV substantially preferred vanillin (8800 s−1·mM−1) over syringaldehyde (1.4 s−1·mM−1). These results clearly demonstrate that desV plays a major role in syringaldehyde catabolism. Phylogenetic analyses showed that DesV-like ALDHs formed a distinct phylogenetic cluster separated from the vanillin dehydrogenase cluster.

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A bacterial aromatic aldehyde dehydrogenase critical for the efficient catabolism of syringaldehyde

Kamimura

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Takahashi

et al. 2017

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“…A transgenic bacterium, PDHV85, was engineered from PDH with pVapoligVABC and pJFV2Z85 inserted. The pVapoligVABC and pJFV2Z85 were previously found to contain all the genes (Masai et al 2002(Masai et al , 2007b(Masai et al , 2012Nelson et al 2003) required to convert vanillin, vanillic acid, and ferulic acid into PDC (unpublished data, Otsuka, Katayama, Masai, Okamura, and Nishimura). The P. putida PpY1100 strain was initially selected because it has the ability to take up many low molecular weight aromatic compounds.…”

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confidence: 97%

Engineered Microbial Production of 2-Pyrone-4,6-Dicarboxylic Acid from Lignin Residues for Use as an Industrial Platform Chemical

Qian¹,

Otsuka²,

Sonoki³

et al. 2016

BioResources

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As one of the most abundant materials in nature, lignin has been used widely in co-generation operations and for fine chemicals and bio-fuels production. These uses, although important, are of relatively low value. Lignin contains many aromatic compounds with useful structures, and it is potentially more profitable to produce high-value fine chemicals from the low-molecular weight lignin fraction while using the high-molecular weight fraction for fuel or other applications. A transgenic P. putida bacterial strain PDHV85 was developed with the capability to convert vanillin, vanillic acid, and syringaldehyde to 2-pyrone-4,6-dicarboxylic acid (PDC), a novel platform chemical that can produce a variety of bio-based polymers. Initial testing with vanillin showed promise for lignin conversion. Testing for this, we used kraft lignin, Japanese cedar (Cryptomeria japonica), or birch (Betula platyphylla) to represent some of the most abundant industrial lignin sources from softwood and hardwood. Repeated manipulation of culture conditions and strain adaptation allowed conversion of these extracts to PDC by PDHV85, which has not previously been reported in a bacterial strain. No inhibition was observed at 0.14 mg/mL kraft lignin extract, 1.14 mg/mL Japanese cedar extract, nor 1.15 mg/mL birch extract when using the optimized growth conditions.

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“…strain SYK-6, is the best-characterized bacterial degrader of lignin-derived aromatic compounds (19). The catabolic pathways and catabolic genes in this strain for ␤-aryl ether (13)(14)(15), biphenyl (20)(21)(22), pinoresinol (23), ferulate (24,25), vanillin (26,27), and syringate (28) have been extensively characterized. However, the catabolic genes for a phenylcoumaran compound, dehydrodiconiferyl alco-hol (DCA), remain largely unknown.…”

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Membrane-Associated Glucose-Methanol-Choline Oxidoreductase Family Enzymes PhcC and PhcD Are Essential for Enantioselective Catabolism of Dehydrodiconiferyl Alcohol

Takahashi

Hirose

Kamimura

et al. 2015

Appl Environ Microbiol

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e Sphingobium sp. strain SYK-6 is able to degrade various lignin-derived biaryls, including a phenylcoumaran-type compound, dehydrodiconiferyl alcohol (DCA). In SYK-6 cells, the alcohol group of the B-ring side chain of DCA is initially oxidized to the carboxyl group to generate 3-(2-(4-hydroxy-3-methoxyphenyl)-3-(hydroxymethyl)-7-methoxy-2,3-dihydrobenzofuran-5-yl) acrylic acid (DCA-C). Next, the alcohol group of the A-ring side chain of DCA-C is oxidized to the carboxyl group, and then the resulting metabolite is catabolized through vanillin and 5-formylferulate. In this study, the genes involved in the conversion of DCA-C were identified and characterized. The DCA-C oxidation activities in SYK-6 were enhanced in the presence of flavin adenine dinucleotide and an artificial electron acceptor and were induced ca. 1.6-fold when the cells were grown with DCA. Based on these observations, SLG_09480 (phcC) and SLG_09500 (phcD), encoding glucose-methanol-choline oxidoreductase family proteins, were presumed to encode DCA-C oxidases. Analyses of phcC and phcD mutants indicated that PhcC and PhcD are essential for the conversion of (؉)-DCA-C and (؊)-DCA-C, respectively. When phcC and phcD were expressed in SYK-6 and Escherichia coli, the gene products were mainly observed in their membrane fractions. The membrane fractions of E. coli that expressed phcC and phcD catalyzed the specific conversion of DCA-C into the corresponding carboxyl derivatives. In the oxidation of DCA-C, PhcC and PhcD effectively utilized ubiquinone derivatives as electron acceptors. Furthermore, the transcription of a putative cytochrome c gene was significantly induced in SYK-6 grown with DCA. The DCA-C oxidation catalyzed by membrane-associated PhcC and PhcD appears to be coupled to the respiratory chain. L ignin, one of the major components of plant cell walls, is a complex phenolic polymer resulting from the oxidative combinatorial coupling of 4-hydroxycinnamyl alcohols (1). Although lignin has various intermolecular linkages between phenylpropane units and contains a number of asymmetric carbons, it is considered to be optically inactive, implying the racemic nature of the lignin backbone (2-4). In nature, lignin is initially decomposed by phenol oxidases such as lignin peroxidase, manganese peroxidase, versatile peroxidase, and laccase secreted by white rot fungi (5-7). Recently, dye-decolorizing peroxidases (Dyp) of Rhodococcus (8) and Amycolatopsis (9) and small laccase of Streptomyces (10) were characterized, and these enzymes have been implicated as being involved in lignin degradation. In addition, bacteria play key roles in the degradation and mineralization of low-molecular-weight aromatic compounds derived from lignin (11, 12). Since fragmented oligomers from lignin consist of stereoisomers that contain various types of intermolecular linkages between phenylpropane units, catabolic enzymes necessary for the conversion of such stereoisomers must have evolved in bacteria to fully utilize structurally and stereochemically complicated l...

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Characterization ofligVEssential for Catabolism of Vanillin bySphingomonas paucimobilisSYK-6

Cited by 60 publications

References 23 publications

A bacterial aromatic aldehyde dehydrogenase critical for the efficient catabolism of syringaldehyde

A bacterial aromatic aldehyde dehydrogenase critical for the efficient catabolism of syringaldehyde

Engineered Microbial Production of 2-Pyrone-4,6-Dicarboxylic Acid from Lignin Residues for Use as an Industrial Platform Chemical

Membrane-Associated Glucose-Methanol-Choline Oxidoreductase Family Enzymes PhcC and PhcD Are Essential for Enantioselective Catabolism of Dehydrodiconiferyl Alcohol

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