The Metabolism of 1‐Phenylethanol and Acetophenone by <i>Nocardia</i> T5 and an <i>Arthrobacter</i> Species

Cripps, R. E.; Trudgill, Peter; Whateley, John G.

doi:10.1111/j.1432-1033.1978.tb12297.x

Cited by 68 publications

(38 citation statements)

References 34 publications

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“…Pseudomonas putida JD1 was maintained on nutrient agar slopes. It was grown in liquid medium containing, per liter, 2.4 g of KH 2 PO 4 , 4.8 g of Na 2 HPO 4 , 2.0 g of NH 4 Cl, 4 ml of salts solution (16), and 0.4 g of 4-hydroxyacetophenone. A large crop of bacteria for enzyme purification was grown by inoculating 10 liters of medium in a New Brunswick laboratory fermentor, stirred at 300 rpm and aerated at a rate of 4 liters/min, with 1 liter of growing culture grown in a conical flask on an orbital incubator at 150 rpm and 30°C.…”

Section: Methodsmentioning

confidence: 99%

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Conversion of 4-Hydroxyacetophenone into 4-Phenyl Acetate by a Flavin Adenine Dinucleotide-Containing Baeyer-Villiger-Type Monooxygenase

Tanner

Hopper

2000

J Bacteriol

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An arylketone monooxygenase was purified from Pseudomonas putida JD1 by ion exchange and affinity chromatography. It had the characteristics of a Baeyer-Villiger-type monooxygenase and converted its substrate, 4-hydroxyacetophenone, into 4-hydroxyphenyl acetate with the consumption of one molecule of oxygen and oxidation of one molecule of NADPH per molecule of substrate. The enzyme was a monomer with an M r of about 70,000 and contained one molecule of flavin adenine dinucleotide (FAD). The enzyme was specific for NADPH as the electron donor, and spectral studies showed rapid reduction of the FAD by NADPH but not by NADH. Other arylketones were substrates, including acetophenone and 4-hydroxypropiophenone, which were converted into phenyl acetate and 4-hydroxyphenyl propionate, respectively. The enzyme displayed MichaelisMenten kinetics with apparent K m values of 47 M for 4-hydroxyacetophenone, 384 M for acetophenone, and 23 M for 4-hydroxypropiophenone. The apparent K m value for NADPH with 4-hydroxyacetophenone as substrate was 17.5 M. The N-terminal sequence did not show any similarity to other proteins, but an internal sequence was very similar to part of the proposed NADPH binding site in the Baeyer-Villiger monooxygenase cyclohexanone monooxygenase from an Acinetobacter sp.One of the strategies used by microorganisms for the aerobic metabolism of ketones in degradative processes is to perform the biological equivalent of the Baeyer-Villiger reaction. This involves the insertion of an oxygen between the keto carbon and an adjacent carbon to form an ester, which can then be readily hydrolyzed. This sequence has been described for the degradation of a number of cyclic ketones, for example cyclohexanone and camphor, which yield lactones on oxygenation (6,20), and for the splitting of aliphatic ketones such as 2-tridecanone (1) or the removal of the side chain of progesterone (13). Several of the enzymes involved in the oxygenating reaction have been purified, and the cyclohexanone monooxygenase from an Acinetobacter species has been studied in great detail and particularly well characterized (2, 7, 21). Generally they have the properties of flavoprotein monooxygenases with a requirement for reduced NAD or NADP, although the enzymes that lactonize the enantiomers of camphor require an additional protein to transfer electrons from the NADH to the monooxygenase component (20). Some of these enzymes have broad substrate specificities, including the ability to oxidize sulfur or selenium atoms in organic compounds, and they are capable of forming chiral products in high enantiomeric excess. Consequently, there has been considerable interest in this class of enzyme because of the potential use for the biological production of chiral synthons, and some of these enzymes are now produced commercially (14,15).In addition to the metabolism of cyclic and aliphatic ketones, the degradation of aryl ketones can also proceed by formation of an ester, apparently by the action of a Baeyer-Villiger type of monooxygenase. In the...

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Section: Methodsmentioning

confidence: 99%

“…In the degradative pathway for acetophenone by an Arthrobacter sp. and by a Nocardia sp., the substrate is oxidized to phenyl acetate (3,4), and a similar route has been proposed for degradation of chlorinated acetophenones by an Alcaligenes sp. and Pseudomonas fluorescens (9).…”

mentioning

confidence: 99%

Conversion of 4-Hydroxyacetophenone into 4-Phenyl Acetate by a Flavin Adenine Dinucleotide-Containing Baeyer-Villiger-Type Monooxygenase

Tanner

Hopper

2000

J Bacteriol

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confidence: 99%

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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“…There is also the possibility that the gentisate pathway genes are linked to a xanthone operon, but are not involved in the degradation of xanthone. This seems unlikely since investigations with several gram-positive and gramnegative aerobic bacteria have indicated fairly tight regulation of aromatic degradative pathways (10,14,20).…”

Section: Discussionmentioning

confidence: 99%

Initial reactions of xanthone biodegradation by an Arthrobacter sp

Tomasek¹,

Crawford²

1986

J Bacteriol

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The Metabolism of 1‐Phenylethanol and Acetophenone by Nocardia T5 and an Arthrobacter Species

Cited by 68 publications

References 34 publications

Conversion of 4-Hydroxyacetophenone into 4-Phenyl Acetate by a Flavin Adenine Dinucleotide-Containing Baeyer-Villiger-Type Monooxygenase

Conversion of 4-Hydroxyacetophenone into 4-Phenyl Acetate by a Flavin Adenine Dinucleotide-Containing Baeyer-Villiger-Type Monooxygenase

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

Initial reactions of xanthone biodegradation by an Arthrobacter sp

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