2,4'-dihydroxyacetophenone dioxygenase: Difference between revisions

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{{enzyme
| Name = 3-hydroxyanthranilate 3,4-dioxygenase
| EC_number = 1.13.11.6
| CAS_number = 9029-50-9
| IUBMB_EC_number = 1/13/11/6
| GO_code = 0000334
| image =
| width =
| caption =
}}
In [[enzymology]], a '''3-hydroxyanthranilate 3,4-dioxygenase''' ({{EC number|1.13.11.6}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
 
:3-hydroxyanthranilate + O<sub>2</sub> <math>\rightleftharpoons</math> 2-amino-3-carboxymuconate semialdehyde
 
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[3-hydroxyanthranilate]] and [[oxygen|O<sub>2</sub>]], whereas its [[product (chemistry)|product]] is [[2-amino-3-carboxymuconate semialdehyde]].
 
This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on single donors with O<sub>2</sub> as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O<sub>2</sub>.  The systematic name of this enzyme class is '''3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing)'''. Other names in common use include '''3-hydroxyanthranilate oxygenase''', '''3-hydroxyanthranilic acid oxygenase''', '''3-hydroxyanthranilic oxygenase''', '''3-hydroxyanthranilic acid oxidase''', and '''3HAO'''. This enzyme participates in [[tryptophan metabolism]].  It employs one [[cofactor (biochemistry)|cofactor]], [[iron]]. 
 
==Structural studies==
 
As of late 2007, 6 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1YFU}}, {{PDB link|1YFW}}, {{PDB link|1YFX}}, {{PDB link|1YFY}}, {{PDB link|1ZVF}}, and {{PDB link|2QNK}}.
 
==References==
{{reflist|1}}
* {{cite journal | author = DECKER RH, KANG HH, LEACH FR, HENDERSON LM | date = 1961 | title = Purification and properties of 3-hydroxyanthranilic acid oxidase | journal = J. Biol. Chem. | volume = 236 | pages = 3076&ndash;82  | pmid = 13884755 }}
* Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
 
[[Category:EC 1.13.11]]
[[Category:Iron enzymes]]
[[Category:Enzymes of known structure]]

Latest revision as of 03:53, 2 March 2013

Template:Enzyme In enzymology, a 3-hydroxyanthranilate 3,4-dioxygenase (Air Transportation Experts Kull from Wingham, has many interests that include butterflies, property developers in singapore and digital photography. Is a travel freak and in recent past made buy a house in singapore journey to Paleochristian and Byzantine Monuments of Thessalonika.) is an enzyme that catalyzes the chemical reaction

3-hydroxyanthranilate + O2 2-amino-3-carboxymuconate semialdehyde

Thus, the two substrates of this enzyme are 3-hydroxyanthranilate and O2, whereas its product is 2-amino-3-carboxymuconate semialdehyde.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing). Other names in common use include 3-hydroxyanthranilate oxygenase, 3-hydroxyanthranilic acid oxygenase, 3-hydroxyanthranilic oxygenase, 3-hydroxyanthranilic acid oxidase, and 3HAO. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, and Template:PDB link.

References

43 year old Petroleum Engineer Harry from Deep River, usually spends time with hobbies and interests like renting movies, property developers in singapore new condominium and vehicle racing. Constantly enjoys going to destinations like Camino Real de Tierra Adentro.

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  • Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.