Catechol 2,3-dioxygenase

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Catechol 2,3-dioxygenase
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Catechol 2,3-dioxygenase tetramer, Pseudomonas alkylphenolica
Identifiers
EC no. 1.13.11.2
CAS no. 9029-46-3
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Catechol 2,3-dioxygenase (EC 1.13.11.2, 2,3-pyrocatechase, catechol 2,3-oxygenase, catechol oxygenase, metapyrocatechase, pyrocatechol 2,3-dioxygenase) is an enzyme with systematic name catechol:oxygen 2,3-oxidoreductase (decyclizing). [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

Degradation of catechol.svg
catechol + O2 2-hydroxymuconate semialdehyde

This enzyme contains Fe(II).

Related Research Articles

An oxygenase is any enzyme that oxidizes a substrate by transferring the oxygen from molecular oxygen O2 (as in air) to it. The oxygenases form a class of oxidoreductases; their EC number is EC 1.13 or EC 1.14.

Catechol dioxygenases are metalloprotein enzymes that carry out the oxidative cleavage of catechols. This class of enzymes incorporate dioxygen into the substrate. Catechol dioxygenases belong to the class of oxidoreductases and have several different substrate specificities, including catechol 1,2-dioxygenase, catechol 2,3-dioxygenase, and protocatechuate 3,4-dioxygenase. The active site of catechol dioxygenases most frequently contains iron, but manganese-containing forms are also known.

<span class="mw-page-title-main">Catechol 1,2-dioxygenase</span> Enzyme

Catechol 1,2- dioxygenase is an enzyme that catalyzes the oxidative ring cleavage of catechol to form cis,cis-muconic acid:

In enzymology, a 2-aminobenzenesulfonate 2,3-dioxygenase (EC 1.14.12.14) is an enzyme that catalyzes the chemical reaction

In enzymology, an anthranilate 1,2-dioxygenase (deaminating, decarboxylating) (EC 1.14.12.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a biphenyl 2,3-dioxygenase (EC 1.14.12.18) is an enzyme that catalyzes the chemical reaction

In enzymology, a terephthalate 1,2-dioxygenase (EC 1.14.12.15) is an enzyme that catalyzes the chemical reaction

In enzymology, a 2,3-dihydroxybenzoate 2,3-dioxygenase (EC 1.13.11.28) is an enzyme that catalyzes the chemical reaction

In enzymology, a 2,3-dihydroxybenzoate 3,4-dioxygenase (EC 1.13.11.14) is an enzyme that catalyzes the chemical reaction

In enzymology, a 2,4'-dihydroxyacetophenone dioxygenase (EC 1.13.11.41) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3,4-dihydroxyphenylacetate 2,3-dioxygenase (EC 1.13.11.15) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-carboxyethylcatechol 2,3-dioxygenase (EC 1.13.11.16) is an enzyme that catalyzes the chemical reaction

Ascorbate 2,3-dioxygenase (EC 1.13.11.13) is an enzyme that catalyzes the chemical reaction

Chloridazon-catechol dioxygenase (EC 1.13.11.36) is an enzyme that catalyzes the chemical reaction

In enzymology, an indole 2,3-dioxygenase (EC 1.13.11.17) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Protocatechuate 3,4-dioxygenase</span>

In enzymology, a protocatechuate 3,4-dioxygenase (EC 1.13.11.3) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Tryptophan 2,3-dioxygenase</span> Mammalian protein found in Homo sapiens

In enzymology, tryptophan 2,3-dioxygenase (EC 1.13.11.11) is a heme enzyme that catalyzes the oxidation of L-tryptophan (L-Trp) to N-formyl-L-kynurenine, as the first and rate-limiting step of the kynurenine pathway.

<span class="mw-page-title-main">Dioxygenase</span> Class of enzymes

Dioxygenases are oxidoreductase enzymes. Aerobic life, from simple single-celled bacteria species to complex eukaryotic organisms, has evolved to depend on the oxidizing power of dioxygen in various metabolic pathways. From energetic adenosine triphosphate (ATP) generation to xenobiotic degradation, the use of dioxygen as a biological oxidant is widespread and varied in the exact mechanism of its use. Enzymes employ many different schemes to use dioxygen, and this largely depends on the substrate and reaction at hand.

<span class="mw-page-title-main">TauD protein domain</span>

In molecular biology, TauD refers to a protein domain that in many enteric bacteria is used to break down taurine as a source of sulfur under stress conditions. In essence, they are domains found in enzymes that provide bacteria with an important nutrient.

Carbazole 1,9a-dioxygenase (EC 1.14.12.22, CARDO) is an enzyme with systematic name 9H-carbazole,NAD(P)H:oxygen oxidoreductase (2,3-hydroxylating). This enzyme catalyses the following chemical reaction

References

  1. Junker F, Field JA, Bangerter F, Ramsteiner K, Kohler HP, Joannou CL, Mason JR, Leisinger T, Cook AM (June 1994). "Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid". The Biochemical Journal. 300 ( Pt 2) (2): 429–36. doi:10.1042/bj3000429. PMC   1138180 . PMID   8002948.
  2. Junker F, Leisinger T, Cook AM (July 1994). "3-Sulphocatechol 2,3-dioxygenase and other dioxygenases (EC 1.13.11.2 and EC 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. strain O-1". Microbiology. 140 ( Pt 7) (7): 1713–22. doi: 10.1099/13500872-140-7-1713 . PMID   8075807.
  3. Hayaishi O, Lardy H, Myrbäck K (1963). "Direct oxygenation by O2, oxygenases". In Boyer PD (ed.). The Enzymes. Vol. 8 (2nd ed.). New York: Academic Press. pp. 353–371.
  4. Kojima Y, Itada N, Hayaishi O (August 1961). "Metapyrocatachase: a new catechol-cleaving enzyme". The Journal of Biological Chemistry. 236: 2223–8. PMID   13757654.
  5. Nozaki M, Kagamiyama H, Hayaishi O (1963). "Metapyrocatechase. I. Purification, Crystallization and Some Properties". Biochemische Zeitschrift. 338: 582–90. PMID   14087325.