hydroxymuconic-semialdehyde and hydroquinone

hydroxymuconic-semialdehyde has been researched along with hydroquinone* in 3 studies

Other Studies

3 other study(ies) available for hydroxymuconic-semialdehyde and hydroquinone

ArticleYear
An unexpected gene cluster for downstream degradation of alkylphenols in Sphingomonas sp. strain TTNP3.
    Applied microbiology and biotechnology, 2012, Volume: 93, Issue:3

    In silico analysis of nucleotide sequences flanking the recently found hydroquinone dioxygenase in Sphingomonas sp. strain TTNP3 revealed a gene cluster that encodes a hydroquinone catabolic pathway. In addition to the two open-reading frames encoding the recently characterized hydroquinone dioxygenase, the cluster consisted of six open-reading frames. We were able to express the three open-reading frames, hqdC, hqdD, and hqdE, and demonstrated that the three gene products, HqdC, HqdD, and HqdE had 4-hydroxymuconic semialdehyde dehydrogenase, maleylacetate reductase, and intradiol dioxygenase activity, respectively. Surprisingly, the gene cluster showed similarities to functionally related clusters found in members of the β- and γ-proteobacteria rather than to those found in other members of the genus Sphingomonas sensu latu.

    Topics: Bacterial Proteins; Biodegradation, Environmental; Biotechnology; Dioxygenases; Fatty Acids, Unsaturated; Genes, Bacterial; Hydroquinones; Molecular Sequence Data; Multigene Family; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Phenols; Sequence Analysis, DNA; Sphingomonas

2012
Hydroquinone dioxygenase from pseudomonas fluorescens ACB: a novel member of the family of nonheme-iron(II)-dependent dioxygenases.
    Journal of bacteriology, 2008, Volume: 190, Issue:15

    Hydroquinone 1,2-dioxygenase (HQDO), an enzyme involved in the catabolism of 4-hydroxyacetophenone in Pseudomonas fluorescens ACB, was purified to apparent homogeneity. Ligandation with 4-hydroxybenzoate prevented the enzyme from irreversible inactivation. HQDO was activated by iron(II) ions and catalyzed the ring fission of a wide range of hydroquinones to the corresponding 4-hydroxymuconic semialdehydes. HQDO was inactivated by 2,2'-dipyridyl, o-phenanthroline, and hydrogen peroxide and inhibited by phenolic compounds. The inhibition with 4-hydroxybenzoate (K(i) = 14 microM) was competitive with hydroquinone. Online size-exclusion chromatography-mass spectrometry revealed that HQDO is an alpha2beta2 heterotetramer of 112.4 kDa, which is composed of an alpha-subunit of 17.8 kDa and a beta-subunit of 38.3 kDa. Each beta-subunit binds one molecule of 4-hydroxybenzoate and one iron(II) ion. N-terminal sequencing and peptide mapping and sequencing based on matrix-assisted laser desorption ionization--two-stage time of flight analysis established that the HQDO subunits are encoded by neighboring open reading frames (hapC and hapD) of a gene cluster, implicated to be involved in 4-hydroxyacetophenone degradation. HQDO is a novel member of the family of nonheme-iron(II)-dependent dioxygenases. The enzyme shows insignificant sequence identity with known dioxygenases.

    Topics: 2,2'-Dipyridyl; Acetophenones; Amino Acid Sequence; Chromatography, Gel; DNA, Bacterial; Enzyme Activators; Enzyme Inhibitors; Enzyme Stability; Fatty Acids, Unsaturated; Hydrogen Peroxide; Hydroquinones; Iron; Mass Spectrometry; Molecular Sequence Data; Molecular Weight; Multigene Family; Open Reading Frames; Oxygenases; Parabens; Phenanthrolines; Protein Subunits; Pseudomonas fluorescens; Sequence Homology, Amino Acid; Substrate Specificity; Temperature

2008
Elucidation of the 4-hydroxyacetophenone catabolic pathway in Pseudomonas fluorescens ACB.
    Journal of bacteriology, 2008, Volume: 190, Issue:15

    The catabolism of 4-hydroxyacetophenone in Pseudomonas fluorescens ACB is known to proceed through the intermediate formation of hydroquinone. Here, we provide evidence that hydroquinone is further degraded through 4-hydroxymuconic semialdehyde and maleylacetate to beta-ketoadipate. The P. fluorescens ACB genes involved in 4-hydroxyacetophenone utilization were cloned and characterized. Sequence analysis of a 15-kb DNA fragment showed the presence of 14 open reading frames containing a gene cluster (hapCDEFGHIBA) of which at least four encoded enzymes are involved in 4-hydroxyacetophenone degradation: 4-hydroxyacetophenone monooxygenase (hapA), 4-hydroxyphenyl acetate hydrolase (hapB), 4-hydroxymuconic semialdehyde dehydrogenase (hapE), and maleylacetate reductase (hapF). In between hapF and hapB, three genes encoding a putative intradiol dioxygenase (hapG), a protein of the Yci1 family (hapH), and a [2Fe-2S] ferredoxin (hapI) were found. Downstream of the hap genes, five open reading frames are situated encoding three putative regulatory proteins (orf10, orf12, and orf13) and two proteins possibly involved in a membrane efflux pump (orf11 and orf14). Upstream of hapE, two genes (hapC and hapD) were present that showed weak similarity with several iron(II)-dependent extradiol dioxygenases. Based on these findings and additional biochemical evidence, it is proposed that the hapC and hapD gene products are involved in the ring cleavage of hydroquinone.

    Topics: Acetophenones; Adipates; Bacterial Proteins; Cloning, Molecular; DNA, Bacterial; Enzymes; Fatty Acids, Unsaturated; Ferredoxins; Hydroquinones; Magnetic Resonance Spectroscopy; Maleates; Membrane Transport Proteins; Metabolic Networks and Pathways; Molecular Sequence Data; Multigene Family; Open Reading Frames; Oxidoreductases Acting on CH-CH Group Donors; Oxygenases; Pseudomonas fluorescens; Sequence Analysis, DNA

2008