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Pseudomonas, pyrocatechase

Circular Dichroism. The circular dichroism (CD) bands of Pseudomonas pyrocatechase can be classified into three groups ... [Pg.157]

Table 4. Substrate specificity of pyrocatechases from Pseudomonas, Brevibacterium and Acinetobactor... Table 4. Substrate specificity of pyrocatechases from Pseudomonas, Brevibacterium and Acinetobactor...
Serological Properties. Antisera prepared against purified preparation of Acineto-bactor pyrocatechase cross-react and inhibit the enzyme activity in the crude extracts prepared from other strains of Acinetobactor calcoaceticus, but fail to cross-react and inhibit isofunctional enzymes prepared from strains of Pseudomonas, Nocardia, and Alcaligenes114. ... [Pg.158]

These enzymes are red in color and contain ferric ion as the sole cofactor. Two types of enzymes have been isolated from various bacteria — pyrocatechases which catalyze catechol cleavage and protocatechuate 3,4-dioxygenases which cleave 3,4-dihydroxybenzoate (protocatechuate). The pyrocatechases have molecular weights in the 60.000-90.000 dalton range9-11) the enzyme from Pseudomonas arvilla (MW 63.000) has two subunits with the molecular form a0Fe9), while the enzyme from Acinetobacter calcoaceticus (MW 85.000) is a dimer of the form (aFe)210). [Pg.40]

Recently, Ques ) reported that when o-aminophenol was added to pyrocatechase from Pseudomonas arvilla, ring cleavage occurred between C-l and C-6 yielding an intermediate which cyclized rapidly to picolinic acid. There was some hydrolysis of the intermediate but no cleavage between C-l and C-2 was observed. [Pg.54]

Beijerinckia sp. B836 Beijerinckia sp. 199 Cunninghamella elegans Pseudomonas putida By consortia of bacteria Pyrocatechase I Achromobacter sp. [Pg.248]

Pseudomonas putida (grown on toluene) unidentified bacterium, strain WR1306 Pyrocatechases... [Pg.248]

Pyrocatechase. Pyrocatechase which catalyzes an oxygenative in-tradiol cleavage of catechol to form cis,cis-muconic acid (Reaction 2), was purified from cells of Pseudomonas arvilla C-1 according to the method previously described (7). The native enzyme was found to con-... [Pg.243]

Phenolytic Oxygenases. In the oxidation of tryptophan by a Pseudomonas an intermediate, catechol, is converted to czs,as-muconic acid by an enzyme named pyrocatechase (VI). This enzyme requires ferrous... [Pg.215]

Pyrocatechase occurs in aerobic microorganisms Pseudomonas, Vdmo, Mycobacterium) as part of a network of enzymes which catalyze the oxidative degradation of aromatic compounds to succinate and acetyl-CoA (Fig. 1) (182,313,433,674,693,698,759). These processes have been extensively studied by means of adaptive phenomena, and by chemical isolation of products formed by living cells (63,234-236,238,291,423,676-678,690, 8). The pyrocatechase step consists in oxidation of catechol to m,m-muconic acid (equation 4), (237,322) ... [Pg.81]

Pyrocatechase has been isolated from Pseudomonas adapted to anthranilic acid or to tryptophan (321,322,591,695,716). The enzyme catalyzes the consumption of one molecule of oxygen per molecule of catechol (CjHjOj) oxidized (321,322) and the product, cis,m-muconic acid (CeH(04), contains two atoms of oxygen more than catechol. [Pg.81]

Pyrocatechase Pseudomonas Catechol cit,c[Pg.12]

Pyrocatechase is an enzyme widely distributed among bacteria. It catalyzes an oxidation of o-dihydroxybenzene, and is named according to the traditional name of the substrate, pyrocatechol. Pyrocatechol, more commonly known by the abbreviated designation catechol, is an intermediate in the metabolism of many aromatic compounds, including mandelic acid, nitrobenzoic acid, anthranilic acid, and other compounds that may be converted to salicylic acid. Benzoic acid and phenol are also precursors of catechol. The best-studied enzyme is that obtained from a strain of Pseudomonas that can use tryptophan as a carbon source. The enzyme is formed adaptively when tryptophan, catechol, or any intermediate between the amino acid and catechol (Fig. 4) is used as a substrate for the cells (Suda et al., 1950). [Pg.89]

The oxidation of tryptophan by various strains of Pseudomonas has been shown to proceed in all cases via kynurine. One sequence of reactions, the aromatic pathway, continues by eliminating the alanine side chain through the action of kynureninase, and subsequently utilizes oxygen for the formation of catechol and the pyrocatechase reaction already discussed. Another pathway retains the side chain of kynurenine and forms kynurenic acid through the action of kynurenine transaminase. A sequence of reactions has been indicated by recent work of Hayaishi and his associates (Kuno et al., 1961) this sequence appears to include three oxygenase reactions one hydroxylation and two phenolytic oxygenations (Fig. 18). [Pg.117]


See other pages where Pseudomonas, pyrocatechase is mentioned: [Pg.153]    [Pg.165]    [Pg.153]    [Pg.165]    [Pg.153]    [Pg.161]    [Pg.164]    [Pg.165]    [Pg.40]    [Pg.54]    [Pg.154]    [Pg.21]   
See also in sourсe #XX -- [ Pg.81 ]




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