THE BACTERIAL DEGRADATION OF CATECHOL.
Ontology highlight
ABSTRACT:
SUBMITTER: DAGLEY S
PROVIDER: S-EPMC1214345 | biostudies-other | 1965 May
REPOSITORIES: biostudies-other
Similar Datasets
Project description:The pathway for biodegradation of benzothiazole (BT) and 2-hydroxybenzothiazole (OBT) by Rhodococcus pyridinovorans strain PA was studied in detail. The kinetics of biodegradation were monitored by in situ (1)H nuclear magnetic resonance (NMR) in parallel with reversed-phase high-performance liquid chromatography (HPLC). Successive oxidations from BT to OBT and then from OBT to dihydroxybenzothiazole were observed. Further insight was obtained by using a mutant strain with impaired ability to grow on BT and OBT. The precise structure of another intermediate was determined by in situ two-dimensional (1)H-(13)C NMR and HPLC-electrospray ionization mass spectrometry; this intermediate was found to be a ring-opening product (a diacid structure). Detection of this metabolite, together with the results obtained by (1)H and (19)F NMR when cells were incubated with 3-fluorocatechol, demonstrated that a catechol 1,2-dioxygenase is involved in a pathway for biodegradation of BTs in this Rhodococcus strain. Our results show that catechol 1,2-dioxygenase and catechol 2,3-dioxygenase activities may both be involved in the biodegradation of BTs depending on the culture conditions.
| S-EPMC134439 | biostudies-literature
Project description:On the basis of the constitutive phenotypes of two catM mutants of Acinetobacter calcoaceticus, the CatM protein was proposed to repress expression of two different loci involved in catechol degradation, catA and catBCIJFD (E. Neidle, C. Hartnett, and L. N. Ornston, J. Bacteriol. 171:5410-5421, 1989). In spite of its proposed negative role as a repressor, CatM is similar in amino acid sequence to positive transcriptional activators of the LysR family. Investigating this anomaly, we found that insertional inactivation of catM did not cause the phenotype expected for the disruption of a repressor-encoding gene: in an interposon-generated catM mutant, no cat genes were expressed constitutively, but rather catA and catB were still inducible by muconate. Moreover, this catM mutant grew poorly on benzoate, a process requiring the expression of all cat genes. The inducibility of the cat genes in this catM mutant was completely eliminated by a 3.5-kbp deletion 10 kbp upstream of catM. In this double mutant, catM in trans restored muconate inducibility to both catA and catB. These results suggested the presence of an additional regulatory locus controlling cat gene expression. The ability of CatM to function as an activator was also suggested by these results. In support of this hypothesis, in vivo methylation protection assays showed that CatM protects two guanines in a dyad 65 nucleotides upstream of the catB transcriptional start site, in a location and pattern typical of LysR-type transcriptional activators. Gel mobility shift assays indicated that CatM also binds to a region upstream of catA. DNA sequence analysis revealed a nucleotide near the 3' end of catM not present in the published sequence. Translation of the corrected sequence resulted in the deduced CatM protein being 52 residues longer than previously reported. The size, amino acid sequence, and mode of action of CatM now appear similar to, and typical of, what has been found for transcriptional activators in the LysR family. Analysis of one of the constitutive alleles of catM previously thought to encode a dysfunctional repressor indicated instead that it encodes an inducer-independent transcriptional activator.
| S-EPMC177415 | biostudies-other
Project description:Compounds containg catechol or bisphosphonate were tested as inhibitors of the zinc metalloproteases, thermolysin (TLN), pseudolysin (PLN) and aureolysin (ALN) which are bacterial virulence factors, and the human matrix metalloproteases MMP-9 and -14. Inhibition of virulence is a putative strategy in the development of antibacterial drugs, but the inhibitors should not interfere with human enzymes. Docking indicated that the inhibitors bound MMP-9 and MMP-14 with the phenyl, biphenyl, chlorophenyl, nitrophenyl or methoxyphenyl ringsystem in the S1'-subpocket, while these ringsystems entered the S2'- or S1 -subpockets or a region involving amino acids in the S1'- and S2'-subpockets of the bacterial enzymes. An arginine conserved among the bacterial enzymes seemed to hinder entrance deeply into the S1'-subpocket. Only the bisphosphonate containing compound RC2 bound stronger to PLN and TLN than to MMP-9 and MMP-14. Docking indicated that the reason was that the conserved arginine (R203 in TLN and R198 in PLN) interacts with phosphate groups of RC2.
| S-EPMC7993378 | biostudies-literature
Project description:Various carcinogens induce EGFR/RAS/MAPK signaling, which is critical in the development of lung cancer. In particular, constitutive activation of extracellular signal-regulated kinase 2 (ERK2) is observed in many lung cancer patients, and therefore developing compounds capable of targeting ERK2 in lung carcinogenesis could be beneficial. We examined the therapeutic effect of catechol in lung cancer treatment. Catechol suppressed anchorage-independent growth of murine KP2 and human H460 lung cancer cell lines in a dose-dependent manner. Catechol inhibited ERK2 kinase activity in vitro, and its direct binding to the ERK2 active site was confirmed by X-ray crystallography. Phosphorylation of c-Myc, a substrate of ERK2, was decreased in catechol-treated lung cancer cells and resulted in reduced protein stability and subsequent down-regulation of total c-Myc. Treatment with catechol induced G1 phase arrest in lung cancer cells and decreased protein expression related to G1-S progression. In addition, we showed that catechol inhibited the growth of both allograft and xenograft lung cancer tumors in vivo. In summary, catechol exerted inhibitory effects on the ERK2/c-Myc signaling axis to reduce lung cancer tumor growth in vitro and in vivo, including a preclinical patient-derived xenograft (PDX) model. These findings suggest that catechol, a natural small molecule, possesses potential as a novel therapeutic agent against lung carcinogenesis in future clinical approaches.
| S-EPMC5085205 | biostudies-literature
Project description:Paracoccus sp. MKU1, a metabolically versatile bacterium that encompasses diverse metabolic pathways in its genome for the degradation of aromatic compounds, was investigated for catechol bioremediation here for the first time to our knowledge. Paracoccus sp. MKU1 degraded catechol at an optimal pH of 7.5 and a temperature of 37 °C, wherein 100 mg/L catechol was completely mineralized in 96 h but required 192 h for complete mineralization of 500 mg/L catechol. While investigating the molecular mechanisms of its degradation potential, it was unveiled that Paracoccus sp. MKU1 employed both the ortho and meta pathways by inducing the expression of catechol 1,2-dioxygenase (C12O) and catechol 2,3-dioxygenase (C23O), respectively. C23O expression at transcriptional levels was significantly more abundant than C12O, which indicated that catechol degradation was primarily mediated by extradiol cleavage by MKU1. Furthermore, poly(MAA-co-BMA)-GO (PGO) microcomposites containing Paracoccus sp. MKU1 were synthesized, which degraded catechol (100 mg/L) completely within 48 h with excellent recycling performance for three cycles. Thus, PGO@Paracoccus microcomposites proved to be efficient in catechol degradation at not only faster rates but also with excellent recycling performances than free cells. These findings accomplish that Paracoccus sp. MKU1 could serve as a potential tool for bioremediation of catechol-polluted industrial wastewater and soil.
| S-EPMC7364705 | biostudies-literature
Project description:Clean water is one of the sustainable development goals. Organic dye is one of the water pollutants affecting water quality. Hence, the conversion of dyes to safer species is crucial for water treatment. The Fenton reaction using Fe as a catalyst is a promising process. However, homogeneous catalysts are normally sensitive, difficult to separate, and burdensome to reuse. Therefore, a catechol-based hypercrosslinked polymer (catechol-HCP) was developed as an inexpensive solid support for Fe (catechol-HCP-Fe) and applied as a heterogenous Fenton catalyst. The good interaction of the catechol moiety with Fe, as well as the porous structure, simple preparation, low cost, and high stability of catechol-HCP, make it beneficial for Fe-loading in the polymer and Fenton reaction utilisation. The catechol-HCP-Fe demonstrated good catalytic activity for methylene blue (MB) degradation in a neutral pH. Complete decolouration of 100 ppm MB could be observed within 25 min. The rate of reaction was influenced by H2O2 concentration, polymer dose, MB concentration, pH, and temperature. The catechol-HCP-Fe could be reused for at least four cycles. The dominant reactive species of the reaction was considered to be singlet oxygen (1O2), and the plausible mechanism of the reaction was proposed.
| S-EPMC9269043 | biostudies-literature
Project description:Chrysene is a high molecular weight (HMW), polycyclic aromatic hydrocarbon (PAH) known for its recalcitrance and carcinogenic properties and sparsely soluble (0.003 mg/L) in aqueous medium. Due to these refractory properties, bioavailability of chrysene is very low and therefore is persistence in the environment escaping the metabolism by microorganisms. However, few bacterial and fungal strains are reported to degrade chrysene, but with lower efficiency, requiring additional/extraneous carbon sources (co-substrates) for it's complete mineralization. In this study, development, enrichment and characterization of bacterial consortium ASDC, consisting of Rhodococcus sp., ASDC1; Bacillus sp. ASDC2; and Burkholderia sp. ASDC3 were reported. Chrysene was utilized as a sole source of carbon and energy by the consortium, having maximum degradation rate of 1.5 mg/L/day and maximum growth rate of 0.125/h, under optimized conditions of pH 7.0, 37°C under aeration of 150 rpm on gyrating shaking. Chrysene degradation was unaffected in presence of other PAHs like pyrene, fluoranthene, naphthalene, phenanthrene, benzene, toluene and xylene, individually as well as in mixture. The results revealed that peptone, ammonium nitrate, sodium succinate have enhanced the chrysene degradation rate during first 24 h of experimentation, which was later on inhibited with increase in incubation time. The chrysene degradation was inhibited by mercury even at lower concentration (1 mM). The results also revealed that SDS has enhanced its degradation by 5.2-fold for initial 24 h of growth, but with increasing in the incubation period, it decreases by 1.2-fold on 7th day of experimentation. The HPLC studies suggested that chrysene was degraded through phthalic acid pathway by the consortium ASDC and the stoichiometric measurements indicated the complete mineralization of chrysene. The flask scale results were validated at simulated microcosm models, where enriched consortium ASDC exhibited maximum degradation (96%) in polluted, non-sterile soil sediment, indicating that consortial strains along with indigenous metabolism showed synergistic metabolism for degradation of chrysene. Thus, the above study revealed the useful enrichment of bacterial community for synergistic degradation of PAHs (chrysene) which could be further exploited for in situ remediation of PAH contaminated sites.
| S-EPMC6036299 | biostudies-literature
Project description:Tarballs are semi-solid blobs of crude-oil formed in marine environment. Microbial degradation of tarballs is poorly understood, though there are indications that tarball-associated microbes can degrade recalcitrant hydrocarbons present in tarballs. In this study, 38 tarball-associated bacteria from Betul beach, Goa, India were initially screened for crude oil degradation. Based on preliminary studies and literature survey, four bacterial strains, Alcanivorax sp. Betul-O, Marinobacter sp. Betul-26, Pseudomonas sp. Betul-14, and Pseudomonas sp. Betul-M were selected for bacterial consortia preparation. Eleven bacterial consortia were prepared and studied for degradation of n-alkanes and polycyclic aromatic hydrocarbon compounds (PAHs) of tarballs based on gravimetric and GC-MS-MS analyses. The bacterial consortia depleted 53.69-97.78% and 22.78-61.98% of n-alkanes and PAH compounds, respectively, within 45 days. Bacterial consortium comprising Pseudomonas sp. Betul-14, Pseudomonas sp. Betul-M, and Alcanivorax sp. Betul-O exhibited promising tarball degradation abilities with 97.78% and 61.98% degradation of n-alkanes and PAH, respectively, within 45 days. Further research is required to obtain insights into degradation products and possible pathways involved.
| S-EPMC7010898 | biostudies-literature
Project description:Chlorophenols (CPs) and their derivatives are persistent environmental pollutants which are used in the manufacture of dyes, drugs, pesticides and other industrial products. CPs, which include monochlorophenols, polychlorophenols, chloronitrophenols, chloroaminophenols and chloromethylphenols, are highly toxic to living beings due to their carcinogenic, mutagenic and cytotoxic properties. Several physico-chemical and biological methods have been used for removal of CPs from the environment. Bacterial degradation has been considered a cost-effective and eco-friendly method of removing CPs from the environment. Several bacteria that use CPs as their sole carbon and energy sources have been isolated and characterized. Additionally, the metabolic pathways for degradation of CPs have been studied in bacteria and the genes and enzymes involved in the degradation of various CPs have been identified and characterized. This review describes the biochemical and genetic basis of the degradation of CPs and their derivatives.
| S-EPMC3975901 | biostudies-other
Project description:The goal of this study is to obtain a genomic view of the Fur regulatory network under both iron replete and iron deficient conditions in Bacillus subtilis using ChIP-seq. Besides the known Fur target sites, 70 putative DNA binding sites were identified, and the vast majority had higher occupancy under iron sufficient conditions. In addition,we discovered a role for catechol degradation in bacillibactin metabolism, and provided evidence that catechol 2,3-dioxygenase can detoxify endogenously produced catechol substrates in addition to its more widely studied role in biodegradation of environmental aromatic compounds and pollutants.
2018-08-29 | GSE119163 | GEO