Degradation of trans-ferulic acid by Pseudomonas acidovorans

Toms, Anne; Wood, John M.

doi:10.1021/bi00804a021

Cited by 132 publications

(73 citation statements)

References 21 publications

(22 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our results cannot identify whether this was due to limiting amounts of NAD in the crude extract or, alternatively, to the presence of an aromatic aldehyde oxidase, as has been reported in Streptomyces viridosporus (Crawford et al, 1982) and in Bacillus subtilis (Gurujeyalakshmi & Mahadevan, 1987). Detection of low levels of protocatechuic acid in the culture medium indicates that in P. fluorescens AN103, further metabolism of vanillic acid occurs via demethoxylation (Brunel & Davison, 1988;Cartwright & Buswell, 1967;Cartwright & Smith, 1967;Ribbons, 1970) followed by an ortho (Omori et al, 1988) or meta (Toms & Wood, 1970) ring cleavage of protocatechuic acid.…”

Section: Discussionmentioning

confidence: 99%

Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens

1998

View full text Add to dashboard Cite

A soil bacterium, designated Pseudomonas fluorescens AN1 03, was isolated based on its ability to grow on ferulic acid as a sole source of carbon and energy. In addition, this strain was found to metabolize a number of related phenolic substrates which contained a hydroxyl group at the para position of the aromatic ring. During growth on ferulic acid, transient accumulation of vanillic acid and trace amounts of protocatechuic acid were detected in the culture medium. Washed cells grown on ferulic acid readily oxidized vanillin, vanillic acid and protocatechuic acid, the three putative intermediates of the metabolic pathway. The side-chain cleavage of ferulic acid to produce vanillin was demonstrated in wifm for the first time and this enzyme-catalysed reaction was shown to have an essential requirement for CoASH, ATP and MgCI,. This conversion involved a two-step process involving a CoA ligase followed by the side-chain cleavage. The addition of NAD increased the oxidation of vanillin to vanillic acid and had an overall effect of increasing the rate of ferulic acid cleavage. The application of 13C-NMR studies in witm revealed acetyl-CoA as the C, side-chain cleavage product. High levels of inducible ferulate-CoA ligase and NAD-linked vanillin dehydrogenase were detected and a novel pathway for ferulic acid metabolism in this organism is proposed.

show abstract

Section: Discussionmentioning

confidence: 99%

Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens

1998

View full text Add to dashboard Cite

show abstract

“…p-Coumarate is also a component of suberin, a polyester polymer located in plant cell walls (10), and it is produced in monomeric form by plants as a defense compound in response to tissue damage (6). Many soil bacteria have a well-developed ability to degrade p-coumarate and two other p-hydroxycinnamates, ferulate and caffeate, under both aerobic and anaerobic conditions (2,3,5,9,12,23,24,26,29,31,40).…”

mentioning

confidence: 99%

Anaerobic p -Coumarate Degradation by Rhodopseudomonas palustris and Identification of CouR, a MarR Repressor Protein That Binds p -Coumaroyl Coenzyme A

et al. 2012

View full text Add to dashboard Cite

The phenylpropanoid p-coumarate and structurally related aromatic compounds are produced in large amounts by green plants and are excellent carbon sources for many soil bacteria. Aerobic bacteria remove the acyl side chain from phenylpropanoids to leave an aromatic aldehyde, which then enters one of several possible central pathways of benzene ring degradation. We investigated the pathway for the anaerobic degradation of p-coumarate by the phototrophic bacterium Rhodopseudomonas palustris and found that it also follows this metabolic logic. We characterized enzymes for the conversion of p-coumarate to p-hydroxybenzaldehyde and acetyl coenzyme A (acetyl-CoA) encoded by the couAB operon. We also identified a MarR family transcriptional regulator that we named CouR. A couR mutant had elevated couAB expression. In addition, His-tagged CouR bound with high affinity to a DNA fragment encompassing the couAB promoter region, and binding was abrogated by the addition of nanomolar quantities of p-coumaroyl-CoA but not by p-coumarate. Footprinting demonstrated binding of CouR to an inverted repeat sequence that overlaps the ؊10 region of the couAB promoter. Our results provide evidence for binding of a CoA-modified aromatic compound by a MarR family member. Although the MarR family is widely distributed in bacteria and archaea and includes over 12,000 members, ligands have been identified for relatively few family members. Here we provide biochemical evidence for a new category of MarR ligand.

show abstract

“…Synthetic vanillin is currently produced from petrochemicals and from lignin (11). Vanillin is also wellknown as a metabolic intermediate in the catabolism of phenolic stilbenes such as eugenol, ferulic acid, and lignin (10,47,51,53). However, the degradation of this widely distributed metabolite has not been examined in detail so far.…”

mentioning

confidence: 99%

Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate

1997

View full text Add to dashboard Cite

The gene loci vdh, vanA, and vanB, which are involved in the bioconversion of vanillin to protocatechuate by Pseudomonas sp. strain HR199 (DSM 7063), were identified as the structural genes of a novel vanillin dehydrogenase (vdh) and the two subunits of a vanillate demethylase (vanA and vanB), respectively. These genes were localized on an EcoRI fragment (E230), which was cloned from a Pseudomonas sp. strain HR199 genomic library in the cosmid pVK100. The vdh gene was identified on a subfragment (HE35) of E230, and the vanA and vanB genes were localized on a different subfragment ( Pseudomonas strains, which were unable to utilize vanillin or vanillate as carbon sources, respectively, conferred the ability to grow on these substrates to these bacteria.Vanillin is one of the most important aromatic flavor compounds in the production of flavors for foods and fragrances for perfumes. Synthetic vanillin is currently produced from petrochemicals and from lignin (11). Vanillin is also wellknown as a metabolic intermediate in the catabolism of phenolic stilbenes such as eugenol, ferulic acid, and lignin (10,47,51,53). However, the degradation of this widely distributed metabolite has not been examined in detail so far.The pathway for the biodegradation of vanillic acid is well understood. The aromatic methyl ether is demethylated via hydroxylation, generating an unstable hemiacetal, which decomposes to protocatechuic acid and formaldehyde (8,9,41,42). The genes vanA and vanB from Pseudomonas sp. strain ATCC 19151, which code for the monooxygenase, which catalyzes this reaction, were cloned and sequenced (5). This vanillate demethylase consisted of two different subunits. The vanB gene product seemed to be related to ferredoxins but was considerably larger. The identity of the vanA gene product remained unknown.In contrast, no molecular data are available for the enzymes catalyzing the conversion of vanillin to vanillate. In the present paper, we describe the cloning, molecular characterization, and heterologous expression of Pseudomonas sp. strain HR199 genes which are responsible for the bioconversion of vanillin to protocatechuate (Fig. 1). MATERIALS AND METHODSBacterial strains and plasmids. The Pseudomonas, Alcaligenes eutrophus, and Escherichia coli strains and the plasmids used in this study are listed in Table 1.Growth of bacteria. Cells of E. coli were grown at 37ЊC in Luria-Bertani (LB) medium or in M9 minimal medium (43). Cells of Pseudomonas and A. eutrophus were grown at 30ЊC either in a nutrient broth (NB) medium (0.8%, wt/vol) (43) or in mineral salts medium (MM) (45) supplemented with carbon sources as indicated in the text. Vanillin, vanillate, and protocatechuate were dissolved in dimethyl sulfoxide and added to the medium at final concentrations of 0.1% (wt/vol). Tetracycline and kanamycin were used at final concentrations of 25 and 300 g/ml, respectively, for the Pseudomonas sp. strains.Nitrosoguanidine mutagenesis. The nitrosoguanidine mutagenesis of the Pseudomonas sp. strains was performed by a mo...

show abstract

Degradation of trans-ferulic acid by Pseudomonas acidovorans

Cited by 132 publications

References 21 publications

Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens

Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens

Anaerobic p -Coumarate Degradation by Rhodopseudomonas palustris and Identification of CouR, a MarR Repressor Protein That Binds p -Coumaroyl Coenzyme A

Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate

Contact Info

Product

Resources

About