The Bacterial Degradation of Catechol

Dagley, S.; Gibson, David T.

doi:10.1042/bj0950466

Cited by 145 publications

(144 citation statements)

References 18 publications

(8 reference statements)

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“…The results presented in Table 7 on the formation of formate in approximately stoicheiometric quantities from 2-hydroxymuconic semialdehyde when NADase-treated extracts were used, indicate that the non NAD+-dependent activity corresponds to the hydrolytic fission of the semialdehyde reported by Dagley and Gibson [5]. The low, non-induced levels of this activity can therefore be ascribed to a 2-hydroxymuconic semialdehyde hydrolase (reaction 11, Fig.2).…”

Section: The Metabolism Of 2-hydroxymuconicmentioning

confidence: 79%

“…Nishizuka et al [4] demonstrated an NADf-dependent conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate (5-oxohex-2-ene-1,6-dioate), whereas Dagley and Gibson [5], and Bayly and Dagley [6], showed that with their strain a hydrolytic fission of the ringcleavage product occurs, yielding formate and 2-0x0-pent-4-enoic acid.The two different pathways reported by these workers possess a common intermediate, 4-hydroxy-2-oxovalerate, but they diverge again as different end products were shown for the enzymatic degradation of this compound. Acetaldehyde and pyruvate were the products resulting from the aldol cleavage of 4-hydroxy-2-oxovalerate reported by Dagley and Gibson [5], whereas acetate and pyruvate were found to be the end products of catechol metabolism in the strain studied by Nishizuka et al [4].…”

Section: Enzymesmentioning

confidence: 99%

“…Only 42 O/, of the substrate was metabolized by the enzyme preparation. Dagley and Gibson [5] reported a 500/, utilization of synthetic 4-hydroxy-2-oxovalerate by a dialysed extract from a pseudomonad, and presumed that only one enantiomorph was attacked by their organism. Other workers have reported 25O/, [9] and 50°/, [7] conversion of the synthetic material to pyruvate using different Pseudonzonas strains.…”

Section: The Formation Of Acetaldehyde and Pyruvate From Synthetic 4-mentioning

confidence: 99%

“…4-Hydroxy-2-oxovalerate was determined after conversion into 4-methyl-2-oxobutyrolactone by heating in 0.83 M HC1 a t 100°C for 5 min [5]. Synthetic 4-hydroxy-2-oxovalerate was used as standard.…”

Section: Physical and Chemical Measurementsmentioning

confidence: 99%

“…4-Oxalocrotonic acid was synthesized by the method of Lapworth [13], and 4-methyl-2-0x0-butyrolactone by the method of Rossi and Schinz [14]. The lactone was hydrolysed to yield 4-hydroxy-2-oxovalerate by the method of Dagley and Gibson [5]. Acetopyruvate was obtained by alkaline hydrolysis of ethyl acetopyruvate [15], prepared according to the method of Marvel and Drager [16].…”

Section: Chemicals and Enzymatic Reagentsmentioning

confidence: 99%

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The meta Cleavage of Catechol by Azotobacter Species

Sala‐Trepat

Evans

1971

European Journal of Biochemistry

300

192

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1. Catechol was metabolized through 2-hydroxymuconic semialdehyde by cell-free extracts of benzoate-grown Azotobacter strains. Some properties of catechol 2,3 oxygenase preparations from Azotobacter vinelandii 206 are described.2 . Two different enzymatic activities able to attack 2-hydroxymuconic semialdehyde have been found in crude extracts from benzoate-grown cells ; one catalyses a hydrolytic release of formate from the semialdehyde and the other a dehydrogenation of this compound to 4-oxalocrotonate. However, the low, non-inducible levels of 2-hydroxymuconic semialdehyde hydrolase activity appear negligible for metabolic purposes and the semialdehyde seems to be dissimilated almost exclusively via 4-oxalocrotonate, by the action of a NAD+-dependent dehydrogenase, in Azotobacter strains.3, A tautomerase activity responsible for the interconversion of the enol and keto forms of 4-oxalocrotonic acid was found in extracts from benzoate-grown cells.4. 4-Oxalocrotonate was stoicheiometrically converted to CO, and 4-hydroxy-2-oxovalerate by a partially purified extract, with the transient formation of a compound that appears to be 2-oxopent-4-enoic acid. The 4-oxalocrotonate decarboxylase activity was stimulated by Mg2+ or Mn2+ ions and was inhibited by EDTA.5. Cell-free extracts from Azotobacter strains converted synthetic 4-hydroxy-2-oxovalerate to acetaldehyde and pyruvate.6. A reaction sequence, termed the 4-oxalocrotonate pathway, for the dissimilation of catechol to acetaldehyde and pyruvate by Azotobacter species is presented. All the enzymes operative in this pathway were inducible, except the 4-hydroxy-2-oxovalerate aldolase. 7. The findings described here are discussed in connection with the two previously reported meta cleavage pathways for the oxidation of catechol in Pseudomonas strains.

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Section: The Metabolism Of 2-hydroxymuconicmentioning

confidence: 79%

Section: Enzymesmentioning

confidence: 99%

Section: The Formation Of Acetaldehyde and Pyruvate From Synthetic 4-mentioning

confidence: 99%

Section: Physical and Chemical Measurementsmentioning

confidence: 99%

Section: Chemicals and Enzymatic Reagentsmentioning

confidence: 99%

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The meta Cleavage of Catechol by Azotobacter Species

Sala‐Trepat

Evans

1971

European Journal of Biochemistry

300

192

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Rational engineering of the TOLmeta-cleavage pathway

Sheridan

Jackson

Regan

et al. 1998

Biotechnol. Bioeng.

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The meta‐cleavage pathway of Pseudomonas putida mt‐2 was simulated using a biochemical systems simulation developed by Regan (1996). A non‐competitive inhibition term for catechol‐2,3‐dioxygenase (C23O) by 2‐OH‐pent‐2,4‐dienoate (Ki = 150 μM) was incorporated into the model. The simulation predicted steady state accumulation levels in the μM range for metabolites pre‐meta‐cleavage, and in the mM range for metabolites post‐meta‐cleavage. The logarithmic gains L[V−i, Xj] and L[X−i, Xj] clearly indicated that the pathway was most sensitive to the concentration of the starting substrate, benzoate, and the first enzyme of the pathway, toluate‐1,2‐dioxygenase (TO). The simulation was validated experimentally; it was found that the amplification of TO increased the steady state flux from 0.024 to 0.091 (mmol/g cell dwt)/h. This resulted in an increased accumulation of a number of the pathway metabolites (intra‐ and extracellularly), especially cis‐diol, 4‐OH‐2‐oxovalerate, and 4‐oxalocrotonate. Metabolic control analysis indicated that C23O was, in fact, the major controling enzymic step of the pathway with a scaled control coefficient of 0.83. The amplification of TO resulted in a shift of some of the control away from C23O. Catechol‐2,3‐dioxygenase, however, remained as the major controling element of the pathway. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58:240–249, 1998.

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Isotopic composition of inorganic carbon as an indicator of benzoate degradation byPseudomonas putida: temperature, growth rate and pH effects

Barth

Kalin

Larkin

et al. 2000

Rapid Commun. Mass Spectrom.

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Degradation experiments of benzoate by Pseudomonas putida resulted in enzymatic carbon isotope fractionations. However, isotopic temperature effects between experiments at 20 and 30 °C were minor. Averages of the last three values of the CO2 isotopic composition (δ13CCO2(g)) were more negative than the initial benzoate δ13C value (−26.2‰ Vienna Pee Dee Belenite (VPDB)) by 3.8, 3.4 and 3.2‰ at 20, 25 and 30 °C, respectively. Although the maximum isotopic temperature difference found was only 0.6‰, more extreme temperature variations may cause larger isotope effects. In order to understand the isotope effects on the total inorganic carbon (TIC), a better measure is to calculate the proportions of the inorganic carbon species (CO2(g), CO2(aq) and HCO3−) and to determine their cumulative δ13CTIC. In all three experiments δ13CTIC was more positive than the initial isotopic composition of the benzoate at a pH of 7. This suggests an uptake of 12C in the biomass in order to match the carbon balance of these closed system experiments. Copyright © 2000 John Wiley & Sons, Ltd.

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The Bacterial Degradation of Catechol

Cited by 145 publications

References 18 publications

The meta Cleavage of Catechol by Azotobacter Species

The meta Cleavage of Catechol by Azotobacter Species

Rational engineering of the TOLmeta-cleavage pathway

Isotopic composition of inorganic carbon as an indicator of benzoate degradation byPseudomonas putida: temperature, growth rate and pH effects

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