Mechanism of the Pyrocatechase Reaction

Hayaishi, Osamu; Katagiri, Masayuki; Rothberg, Simon

doi:10.1021/ja01625a095

Cited by 334 publications

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“…Absorption spectrum in 0.01 M potassium phosphate buffer, pH 7.0, had a maximum a t 257.5 nm (log E = 4.17). These data are in agreement with the properties of &,cis-muconate, the product of catechol oxidation by catechol 1,2-oxygenase obtained from other microorganisms [4]. On the basis of these results, we consider the enzyme investigated by us as identical with catechol 1,2-oxygenase.…”

Section: Purification Of Catechol 12-0xygenasesupporting

confidence: 89%

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Purification and Properties of Catechol 1,2‐Oxygenase from Trichosporon cutaneum

Várga

Neujahr

1970

European Journal of Biochemistry

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A highly purified preparation of catechol 1,2-oxygenase was obtained from a strain of Trichosporon cutaneum, isolated from soil as a predominant phenol utilizing yeast. The purified active enzyme was homogeneous upon polyacrylamide gel electrophoresis. The enzyme was gradually inactivated upon storage. The inactivation was followed by the appearance of a second, electrophoretically distinct band. The active enzyme is red, the inactive form is colourless. Its molecular weight is 109000 as determined by gel filtration; pH optimum 8.2. The Michaelis constants are 5.9 pM for catechol and 81 pM for oxygen. There is no cofactor requirement for activity. The enzyme is sensitive to iron chelating agents, reducing agents and quinones. The enzyme has a broad substrate specificity: besides catechol it is able to cleave hydroxyl-and methyl-substituted catechols. Several catechol derivatives inhibit the enzyme activity towards catechol.Catechol 1,2-oxygenase was originally purified from a Pseudomonas, and it was proved to be a dioxygenase, which introduces molecular oxygen directly into catechol, with the formation of cispismuconic acid [I-41. Recently the enzyme was isolated from Brevibacterium fuscurn [5]. The molecular weight of the catechol I ,2-oxygenases purified hitherto, is in the range of 70000-100000. The active enzymes are reported to have distinct red colour, and to be non-heme iron proteins.I n a previous work we reported the results of studies on the decomposition of phenols by Trichosporon cutaneum, a yeast isolated by us from soil [6,7]. Results of respirometric studies on intact cells and cell-free preparations indicated that cells adapted to either phenol or resorcinol contained ring cleaving enzyme(s) able to act on catechol and different catechol derivatives. This phenomenon might have been attributed to the presence of Werent ring cleaving enzymes, induced by phenol or resorcinol, as well as to a single enzyme with broad substratespecificity. We wanted to answer this question by purification and characterization of catechol 1,Zoxygenase from T . cutaneum.

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Section: Purification Of Catechol 12-0xygenasesupporting

confidence: 89%

“…The catechol 1,2-oxygenase isolated by us from T. cutaneum exhibits the following similarities and differences in comparison with similar enzymes isolated from other microorganisms [4,16,17]. The mol-ecular weight is of the same order of magnitude (close to 100000).…”

Section: Discussionmentioning

confidence: 73%

Purification and Properties of Catechol 1,2‐Oxygenase from Trichosporon cutaneum

Várga

Neujahr

1970

European Journal of Biochemistry

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“…It had been considered that the oxygen molecule is a terminal electron acceptor and is not incorporated into substrates. By the use of 18 O 2 and H 2 18 O in the reaction catalysed by mushroom phenolase, Howard S. Mason and his coworkers demonstrated the incorporation of an oxygen atom from molecular oxygen into 3,4-dimethylphenol, producing 4,5-dimethylcatechol (1). Concurrently, Osamu Hayaishi and his collaborators found that pseudomonad pyrocatechase incorporated two atoms of oxygen from 18 O 2 (but not from H 2…”

mentioning

confidence: 99%

“…O) into catechol and produced cis,cis-muconic acid (2). At a Symposium on 'Enzymatic Activation of Molecular Oxygen' held at Atlantic City in 1956, Mason proposed the terms oxygen transferase and mixed-function oxidase for the enzymes incorporating two atoms and only one atom of molecular oxygen, respectively.…”

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confidence: 99%

The 50th anniversary of the discovery of oxygenases

Yamamoto

2006

IUBMB Life

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“…oxidoreductase (decyclizing), EC 1.13.11.1), is an intradiol enzyme which catalyzes the conversion of catechol to cis, cis-muconic acid, and contains a ferric form of iron as its sole cofactor (1,2). The C120s studied so far all consist of identical subunits, with the exception of the enzyme obtained from…”

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confidence: 99%

Amino acid sequence of catechol 1,2‐dioxygenase (pyrocatechase) isozyme αα from Pseudomonas arvilla C‐1

et al. 1996

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SummaryCatechol 1,2-dioxygenase catalyzes the oxygenative ring cleavage of catechol to form cis, cis-muconic acid, and contains a ferric form of iron as its sole cofactor. Pseudomonas arvilla C-1 contains three isozymes of the enzyme, a•, cz [3, and [3[3 [C. Nakai et al. (1990) Biol. Chem. 265, 660-665]. We have determined the amino acid sequence of the aa isozyme by direct analysis. The sequence shared 77% homology with isozyme N3, and had conserved tyrosyl and histidyl residues which are thought to be involved in the binding of ferric ion.

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Mechanism of the Pyrocatechase Reaction

Cited by 334 publications

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Purification and Properties of Catechol 1,2‐Oxygenase from Trichosporon cutaneum

Purification and Properties of Catechol 1,2‐Oxygenase from Trichosporon cutaneum

The 50th anniversary of the discovery of oxygenases

Amino acid sequence of catechol 1,2‐dioxygenase (pyrocatechase) isozyme αα from Pseudomonas arvilla C‐1

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