The Catabolism of 4-Hydroxyacetophenone by an Alcaligenes sp.

Hopper, David J.; Jones, H. Gwyn; Elmorsi, Elmorsi A.; Rhodes-Roberts, Muriel E.

doi:10.1099/00221287-131-7-1807

Cited by 18 publications

(21 citation statements)

References 15 publications

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“…4HAP degrades 4-hydroxyacetophenone via DHAP, and the DAD of strain 4HAP is involved in 4-hydroxyacetophenone degradation. 13) On the other hand, the DHAP-degrading bacterium Burkholderia sp. AZ11 did not grow on 4-hydroxyacetophenone.…”

Section: Discussionmentioning

confidence: 99%

“…4HAP grown on 4-hydroxyacetophenone does not degrade hydroquinone, but oxidizes DHAP to 4-hydroxybenzoate. 12,13) In this strain, a hydroxylase converts 4-hydroxyacetophenone to DHAP, and then DHAP dioxygenase (DAD, EC 1.13.11.41) cleaves the hydroxyacetyl group of DHAP to yield 4-hydroxybenzoate and formate. DAD adds the two oxygen atoms of O 2 into two cleavage products one by one.…”

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Molecular and Catalytic Properties of 2,4′-Dihydroxyacetophenone Dioxygenase fromBurkholderiasp. AZ11

Enya

Aoyagi

Hishikawa

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Molecular and Catalytic Properties of 2,4′-Dihydroxyacetophenone Dioxygenase fromBurkholderiasp. AZ11

Enya

Aoyagi

Hishikawa

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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“…4-Hydroxyacetophenone can be converted in two different ways to 4-hydroxybenzoate (28,35,48). The latter compound then enters the ␤-ketoadipate pathway via the formation of the ring cleavage substrate 3,4-dihydroxybenzoate (42).…”

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Elucidation of the 4-Hydroxyacetophenone Catabolic Pathway in Pseudomonas fluorescens ACB

et al. 2008

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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 ␤-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.

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Hydroquinone Dioxygenase from Pseudomonas fluorescens ACB: a Novel Member of the Family of Nonheme-Iron(II)-Dependent Dioxygenases

et al. 2008

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Several aerobic microorganisms are capable of utilizing acetophenones for their growth (16,17,(30)(31)(32). However, relatively little is known about the oxidative enzymes involved in acetophenone mineralization (45,47). The catabolism of 4-hydroxyacetophenone in Pseudomonas fluorescens ACB proceeds through the initial formation of 4-hydroxyphenyl acetate and hydroquinone (31,37,47). The latter compound is further degraded via 4-hydroxymuconic semialdehyde and maleylacetate to ␤-ketoadipate (46). We have purified HapA, the enzyme responsible for the Baeyer-Villiger oxidation of 4-hydroxyacetophenone, and expressed its gene in Escherichia coli (37). Moreover, we established that this flavin adenine dinucleotide-containing monooxygenase is useful for the production of phenols and catechols, which are valuable intermediates in the synthesis of pharmaceuticals, agricultural chemicals, and material products (36,38,48).In the accompanying paper (46), we showed that the genes encoding 4-hydroxyacetophenone monooxygenase (hapA), 4-hydroxyphenylacetate esterase (hapB), 4-hydroxymuconic semialdehyde dehydrogenase (hapE), and maleylacetate reductase (hapF) belong to a gene cluster (hapCDEFGHIBA) involved in 4-hydroxyacetophenone utilization. Based on biochemical data and sequence analysis, we proposed that the function of the hapC and hapD genes is linked to the conversion of hydroquinone to 4-hydroxymuconic semialdehyde.Several ring cleavage enzymes acting on substituted hydroquinones have been described. These include intradiol dioxygenases acting on hydroxyhydroquinone (4,20,22,35,39,42,55,66) and extradiol dioxygenases that are active with (homo-)gentisate (3, 28) or chlorohydroquinone (10,44,51). However, enzymes that use hydroquinone as the physiological ring cleavage substrate have not been characterized. Here we report on the purification and properties of hydroquinone dioxygenase (HQDO) from P. fluorescens ACB. It is shown that the heterotetrameric enzyme, encoded by the hapC and hapD genes, is a novel member of the family of nonheme-iron(II)-dependent dioxygenases. The present results confirm that the hapG gene, encoding an intradiol dioxygenase (46), is not involved in 4-hydroxyacetophenone degradation. This finding has important implications for the function of related genes involved in the catabolism of other aromatic compounds.

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The Catabolism of 4-Hydroxyacetophenone by an Alcaligenes sp.

Cited by 18 publications

References 15 publications

Molecular and Catalytic Properties of 2,4′-Dihydroxyacetophenone Dioxygenase fromBurkholderiasp. AZ11

Molecular and Catalytic Properties of 2,4′-Dihydroxyacetophenone Dioxygenase fromBurkholderiasp. AZ11

Elucidation of the 4-Hydroxyacetophenone Catabolic Pathway in Pseudomonas fluorescens ACB

Hydroquinone Dioxygenase from Pseudomonas fluorescens ACB: a Novel Member of the Family of Nonheme-Iron(II)-Dependent Dioxygenases

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