Purification and characterization of phthalate oxygenase and phthalate oxygenase reductase from Pseudomonas cepacia.

Batie, Christopher J.; LaHaie, E; Ballou, David P.

doi:10.1016/s0021-9258(19)75664-6

Cited by 205 publications

(73 citation statements)

References 56 publications

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“…The m/z value of phthalate was 158.92. Overall, the tR and an m/z values are consistent with the product being cis-4,5-dihydrodiol phthalate (20). The identity of the product was further confirmed by its transformation to protocatechuate by PhtCD as described below.…”

Section: Purification and Biochemical Activitysupporting

confidence: 60%

“…Structural studies on ROs such as naphthalene dioxygenase (NDO) ( 10 , 15 , 16 , 17 , 18 , 19 ) have identified key features that are responsible for substrate specificity and have provided valuable insight into the catalytic mechanism of these enzymes ( 12 ). For example, a small N-terminal domain harbors the [2Fe-2S] cluster while the catalytic center occurs in a larger C-terminal domain ( 20 ). All ROs characterized to date are either α 3 trimers or have an additional small subunit to form an α 3 β 3 hexamer.…”

mentioning

confidence: 99%

“…PDR contains a flavin mononucleotide and a ferredoxin-type [2Fe-2S] center ( 21 ). Work on PDO DB01 pioneered our understanding of RO function ( 11 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 ). For example, these studies were the first to establish that ROs are iron-dependent ( 20 ).…”

mentioning

confidence: 99%

“…Work on PDO DB01 pioneered our understanding of RO function ( 11 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 ). For example, these studies were the first to establish that ROs are iron-dependent ( 20 ). Similarly, ENDOR spectroscopy of the PDO Rieske center provided the first evidence that one of the cluster irons has bis-thiolate coordination while the other has bis-imidazole coordination ( 31 ).…”

mentioning

confidence: 99%

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Molecular insights into substrate recognition and catalysis by phthalate dioxygenase from Comamonas testosteroni

Mahto

Neetu

Waghmode

et al. 2021

Journal of Biological Chemistry

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Phthalate, a plasticizer, endocrine disruptor, and potential carcinogen, is degraded by a variety of bacteria. This degradation is initiated by phthalate dioxygenase (PDO), a Rieske oxygenase (RO) that catalyzes the dihydroxylation of phthalate to a dihydrodiol. PDO has long served as a model for understanding ROs despite a lack of structural data. Here we purified PDO KF1 from Comamonas testosteroni KF1 and found that it had an apparent k cat / K m for phthalate of 0.58 ± 0.09 μM −1 s −1 , over 25-fold greater than for terephthalate. The crystal structure of the enzyme at 2.1 Å resolution revealed that it is a hexamer comprising two stacked α 3 trimers, a configuration not previously observed in RO crystal structures. We show that within each trimer, the protomers adopt a head-to-tail configuration typical of ROs. The stacking of the trimers is stabilized by two extended helices, which make the catalytic domain of PDO KF1 larger than that of other characterized ROs. Complexes of PDO KF1 with phthalate and terephthalate revealed that Arg207 and Arg244, two residues on one face of the active site, position these substrates for regiospecific hydroxylation. Consistent with their roles as determinants of substrate specificity, substitution of either residue with alanine yielded variants that did not detectably turnover phthalate. Together, these results provide critical insights into a pollutant-degrading enzyme that has served as a paradigm for ROs and facilitate the engineering of this enzyme for bioremediation and biocatalytic applications.

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Section: Purification and Biochemical Activitysupporting

confidence: 60%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Molecular insights into substrate recognition and catalysis by phthalate dioxygenase from Comamonas testosteroni

Mahto

Neetu

Waghmode

et al. 2021

Journal of Biological Chemistry

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“…Las oxigenasas Rieske/mononuclear están ampliamente distribuidas en bacterias (proteobacterias, actinobacterias, algunas cianobacterias y firmicutes) e incluso en algunas arqueas (Chakraborty et al, 2012) se ha descrito que estas enzimas están presentes también en bacterias termófilas, sin embargo, hasta el momento no se ha reportado la función de alguna de ellas (Chakraborty, Suzuki-Minakuchi, Okada & Nojiri, 2017). La mayoría de las oxigenasas Rieske/mononuclear presentes en bacterias participan en rutas de degradación de compuestos aromáticos policíclicos, como el naftaleno (Ensley, Gibson, & Laborde, 1982;, carbazol (Sato et al, 1997), bifenil (Haddock & Gibson, 1995), benzoato (Wolfe et al, 2002), cumeno (Dong et al, 2005), oxoquinolina (Rosche, Tshisuaka, Fetzner & Lingens, 1995), ftalato (Batie, Lahaie & Ballous, 1987), benzeno (Mason, Butler, Cammack & Shergill, 1997), tolueno (Jiang, Parales, & Gibson, 1999), entre otros. También se han encontrado oxigenasas Rieske/mononuclear en bacterias que oxidan compuestos no aromáticos como la glicina betaína (Shao, Guo, Zhang, Yu, Zhao & Pang, 2018), el cloruro de benzalconio (Ertekin, Konstantinidis & Tezel, 2017), la prolina betaína (Daughtry et al, 2012) y la carnitina (Zhu et al, 2014).…”

Section: Clasificación Y Distribución Filogenética De Las Oxigenasas Rieske/mononuclearunclassified

Estructura y función de las oxigenasas tipo Rieske/mononuclear

Carrillo-Campos

2019

TIP RECQB

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Las oxigenasas Rieske/mononuclear son un grupo de metaloenzimas que catalizan la oxidación de una variedad de compuestos, destaca su participación en la degradación de compuestos xenobióticos contaminantes; estas enzimas también participan en la biosíntesis de algunos compuestos de interés comercial. Poseen una amplia especificidad por el sustrato, convirtiéndolas en un grupo de enzimas con un alto potencial de aplicación en procesos biotecnológicos que hasta el momento no ha sido explotado. La presente revisión aborda aspectos generales acerca de la función y estructura de este importante grupo de enzimas.

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Effect of inducer addition on production of 4,5-dihydroxyphthalate byPseudomonas testosteroni

Sakurai¹,

Sakakibara²

2000

J. Chem. Technol. Biotechnol.

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The effect of the addition method of an inducer (o-phthalate) for the enhancement of 4,5-dihydroxyphthalate (DHP) production was examined using Pseudomonas testosteroni. The reduction of the lag phase seen when inducer was added in the ®rst 10 h of growth culture did not affect the maximum production rate of DHP. The optimal inducer concentration was about 2 g dm À3 and the rate of DHP production was about four times higher that achieved in the absence of inducer. The fed-batch production of DHP was also carried out and 8 g dm À3 of DHP was obtained.

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Purification and characterization of phthalate oxygenase and phthalate oxygenase reductase from Pseudomonas cepacia.

Cited by 205 publications

References 56 publications

Molecular insights into substrate recognition and catalysis by phthalate dioxygenase from Comamonas testosteroni

Molecular insights into substrate recognition and catalysis by phthalate dioxygenase from Comamonas testosteroni

Estructura y función de las oxigenasas tipo Rieske/mononuclear

Effect of inducer addition on production of 4,5-dihydroxyphthalate byPseudomonas testosteroni

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