Catechol 1,2-Dioxygenase is an Analogue of Homogentisate 1,2-Dioxygenase in Pseudomonas chlororaphis Strain UFB2

Setlhare, Boitumelo; Kumar, Ajit; Mokoena, Mduduzi P.; Olaniran, Ademola O.

doi:10.3390/ijms20010061

Cited by 24 publications

(15 citation statements)

References 33 publications

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“…The samples underwent thorough assessment on a tensile tester, mapping the entire cartilage surface of the tibial plateaus, leading to a similarly wide range of apparent moduli observed. The apparent equilibrium modulus within this work of 0.82 MPa is in line with the work of Kumar et al, showing an average equilibrium modulus of 0.9 MPa in moderately degraded cartilage (ICRS grade III) [ 16 ].…”

Section: Discussionsupporting

confidence: 91%

Can sodium MRI be used as a method for mapping of cartilage stiffness?

Brinkhof

Froeling

Ito

et al. 2020

Magn Reson Mater Phy

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Objective Sodium concentration is responsible for (at least part of) the stiffness of articular cartilage due to the osmotic pressure it generates. Therefore, we hypothesized that we could use sodium MRI to approximate the stiffness of cartilage to assess early cartilage degeneration. Methods Four human tibial plateaus were retrieved from patients undergoing total knee replacement (TKR), and their cartilage stiffness mapped with indentation testing, after which samples were scanned in a 7 T MRI to determine sodium concentration. The relation of biomechanical parameters to MRI sodium and glycosaminoglycan (GAG) concentration was explored by a linear mixed model. Results Weak correlations of GAG concentration with apparent peak modulus (p = 0.0057) and apparent equilibrium modulus (p = 0.0181) were observed and lack of correlation of GAG concentration versus MRI sodium concentration was observed. MRI sodium concentration was not correlated with apparent peak modulus, though a moderate correlation of MRI sodium concentration with permeability was shown (p = 0.0014). Discussion and conclusion Although there was correlation between GAG concentration and cartilage stiffness, this was not similar with sodium concentration as measured by MRI. Thus, if the correlation between MRI sodium imaging and GAG concentration could be resolved, this strategy for assessing cartilage functional quality still holds promise.

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Section: Discussionsupporting

confidence: 91%

Can sodium MRI be used as a method for mapping of cartilage stiffness?

Brinkhof

Froeling

Ito

et al. 2020

Magn Reson Mater Phy

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“…The first C12DO purified was obtained from Pseudomonas fluorescens (Hayaishi et al, 1957) followed by C12DO of Pseudomonas arvilla C-1 (Pseudomonas putida) (Nakai et al, 1979), this last have two non-identical subunits α and β of C12DO, that can form homo-and hetero-dimers (Nakai et al, 1979(Nakai et al, , 1990. In some strains of Pseudomonas genus, exist just one copy of C12DO as in the case of Pseudomonas chlororaphis strain UFB2 and Pseudomonas aeruginosa TKU002, where some characteristics as size (smaller size in C12DO from P. aeruginosa TKU002 22 kDa) and substrate specificity varies, but the dimeric arrangement is highly preserved (Wang et al, 2006;Setlhare et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Novel Functional Trimeric Catechol 1,2-Dioxygenase From a Pseudomonas stutzeri Isolated From the Gulf of Mexico

et al. 2020

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Catechol 1,2 dioxygenases (C12DOs) have been studied for its ability to cleavage the benzene ring of catechol, the main intermediate in the degradation of aromatic compounds derived from aerobic degradation of hydrocarbons. Here we report the genome sequence of the marine bacterium Pseudomonas stutzeri GOM2, isolated from the southwestern Gulf of Mexico, and the biochemical characterization of its C12DO (PsC12DO). The catA gene, encoding PsC12DO of 312 amino acid residues, was cloned and expressed in Escherichia coli. Many C12DOs have been described as dimeric enzymes including those present in Pseudomonas species. The purified PsC12DO enzyme was found as an active trimer, with a molecular mass of 107 kDa. Increasing NaCl concentration in the enzyme reaction gradually reduced activity; in high salt concentrations (0.7 M NaCl) quaternary structural analysis determined that the enzyme changes to a dimeric arrangement and causes a 51% decrease in specific activity on catechol substrate. In comparison with other C12DOs, our enzyme showed a broad range of action for PsC12DO in solutions with pH values ranging from neutral to alkaline (70%). The enzyme is still active after incubation at 50 • C for 30 min and in low temperatures to long term storage after 6 weeks at 4 • C (61%). EDTA or Ca 2+ inhibitors cause no drastic changes on residual activity; nevertheless, the activity of the enzyme was affected by metal ions Fe 3+ , Zn 2+ and was completely inhibited by Hg 2+ . Under optimal conditions the k cat and K m values were 16.13 s −1 and 13.2 µM, respectively. To our knowledge, this is the first report describing the characterization of a marine C12DOs from P. stutzeri isolated from the Gulf of Mexico that is active in a trimeric state. We consider that our enzyme has important features to be used in environments in presence of EDTA, metals and salinity conditions.

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“…A number of aerobic biodegradation pathways of aromatic compounds like benzoate, aniline, phenol, pyrene and naphthalene converge at the catechol ring cleavage reaction, and eventually generate intermediates of the tricarboxylic acid cycle through two different routes [1][2][3]. The catechol meta-cleavage pathway is usually encoded by the nah and xyl genes on plasmids, while the catechol ortho-cleavage pathway is usually determined by the chromosomal cat and ben genes [4][5][6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Function and Molecular Ecology Significance of Two Catechol-Degrading Gene Clusters in Pseudomonas putida ND6

Shi

Liu

Yang

et al. 2021

J. Microbiol. Biotechnol.

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Many bacteria metabolize aromatic compounds via catechol as a catabolic intermediate, and possess multiple genes or clusters encoding catechol-cleavage enzymes. The presence of multiple isozyme-encoding genes is a widespread phenomenon that seems to give the carrying strains a selective advantage in the natural environment over those with only a single copy. In the naphthalene-degrading strain Pseudomonas putida ND6, catechol can be converted into intermediates of the tricarboxylic acid cycle via either the orthoor meta-cleavage pathways. In this study, we demonstrated that the catechol ortho-cleavage pathway genes (catB I C I A I and catB II C II A II) on the chromosome play an important role. The cat I and cat II operons are co-transcribed, whereas catA I and catA II are under independent transcriptional regulation. We examined the binding of regulatory proteins to promoters. In the presence of cis-cis-muconate, a well-studied inducer of the cat gene cluster, CatR I and CatR II occupy an additional downstream site, designated as the activation binding site. Notably, CatR I binds to both the cat I and cat II promoters with high affinity, while CatR II binds weakly. This is likely caused by a T to G mutation in the G/T-N 11-A motif. Specifically, we found that CatR I and CatR II regulate catB I C I A I and catB II C II A II in a cooperative manner, which provides new insights into naphthalene degradation.

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Catechol 1,2-Dioxygenase is an Analogue of Homogentisate 1,2-Dioxygenase in Pseudomonas chlororaphis Strain UFB2

Cited by 24 publications

References 33 publications

Can sodium MRI be used as a method for mapping of cartilage stiffness?

Can sodium MRI be used as a method for mapping of cartilage stiffness?

Characterization of a Novel Functional Trimeric Catechol 1,2-Dioxygenase From a Pseudomonas stutzeri Isolated From the Gulf of Mexico

Function and Molecular Ecology Significance of Two Catechol-Degrading Gene Clusters in Pseudomonas putida ND6

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