5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase: Difference between revisions

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{{enzyme
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| Name = Aldehyde ferredoxin oxidoreductase
| EC_number = 1.2.7.5
| CAS_number = 138066-90-7
| IUBMB_EC_number = 1/2/7/5
| GO_code =
| image =
| width =
| caption =
}}
{{Infobox protein family
| Symbol = AFOR_N
| Name = AFOR_N
| image = PDB 1aor EBI.jpg
| width =
| caption = structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
| Pfam = PF02730
| Pfam_clan = 
| InterPro = IPR013983
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1aor
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
{{Infobox protein family
| Symbol = AFOR_C
| Name = AFOR_C
| Pfam = PF01314
| Pfam_clan = 
| InterPro = IPR001203
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1aor
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
In [[enzymology]], an '''aldehyde ferredoxin oxidoreductase''' ({{EC number|1.2.7.5}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
 
:an aldehyde + H<sub>2</sub>O + 2 oxidized ferredoxin <math>\rightleftharpoons</math> an acid + 2 H<sup>+</sup> + 2 reduced ferredoxin
 
The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[aldehyde]], [[water|H<sub>2</sub>O]], and [[oxidized ferredoxin]], whereas its 3 [[product (chemistry)|products]] are [[acid]], [[hydrogen ion|H<sup>+</sup>]], and [[reduced ferredoxin]].
 
This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor.  The systematic name of this enzyme class is '''aldehyde:ferredoxin oxidoreductase'''. This enzyme is also called '''AOR'''. 
 
[[Enzyme]]s of the aldehyde [[ferredoxin]] [[oxidoreductase]] (AOR) family contain a [[tungsten]] [[cofactor (biochemistry)|cofactor]] and an 4Fe4S cluster.<ref name="pmid9242907">{{cite journal | author = Kisker C, Schindelin H, Rees DC | title = Molybdenum-cofactor-containing enzymes: structure and mechanism | journal = Annu. Rev. Biochem. | volume = 66 | issue = | pages = 233–67 | year = 1997 | pmid = 9242907 | doi = 10.1146/annurev.biochem.66.1.233 | url = }}</ref><ref name="pmid8672295">{{cite journal | author = Kletzin A, Adams MW | title = Tungsten in biological systems | journal = FEMS Microbiol. Rev. | volume = 18 | issue = 1 | pages = 5–63 |date=March 1996 | pmid = 8672295 | doi = | url = }}</ref> This family includes AOR, formaldehyde ferredoxin oxidoreductase (FOR), [[glyceraldehyde-3-phosphate]] ferredoxin oxidoreductase (GAPOR), all isolated from hyperthermophilic [[archea]];<ref name="pmid9242907"/> [[carboxylic acid]] [[reductase]] found in clostridia;<ref name="pmid2550230">{{cite journal | author = White H, Strobl G, Feicht R, Simon H | title = Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes | journal = Eur. J. Biochem. | volume = 184 | issue = 1 | pages = 89–96 |date=September 1989 | pmid = 2550230 | doi = 10.1111/j.1432-1033.1989.tb14993.x| url = }}</ref> and hydroxycarboxylate viologen oxidoreductase from ''Proteus vulgaris'', the sole member of the AOR family containing molybdenum.<ref name="pmid8026480">{{cite journal | author = Trautwein T, Krauss F, Lottspeich F, Simon H | title = The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein | journal = Eur. J. Biochem. | volume = 222 | issue = 3 | pages = 1025–32 |date=June 1994 | pmid = 8026480 | doi = 10.1111/j.1432-1033.1994.tb18954.x| url = }}</ref> GAPOR may be involved in [[glycolysis]],<ref name="pmid7721730">{{cite journal | author = Mukund S, Adams MW | title = Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus | journal = J. Biol. Chem. | volume = 270 | issue = 15 | pages = 8389–92 |date=April 1995 | pmid = 7721730 | doi = 10.1074/jbc.270.15.8389| url = }}</ref> but the functions of the other [[protein]]s are not yet clear. AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid [[oxidoreductases]].<ref name="pmid9275170">{{cite journal | author = Ma K, Hutchins A, Sung SJ, Adams MW | title = Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 94 | issue = 18 | pages = 9608–13 |date=September 1997 | pmid = 9275170 | pmc = 23233 | doi = 10.1073/pnas.94.18.9608| url = }}</ref>
 
==References==
{{reflist}}
 
==Further reading==
{{reflist}}
* {{cite journal | author = Mukund S, Adams MW | year = 1991 | title = The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway | journal = J. Biol. Chem.  | volume = 266 | pages = 14208&ndash;16  | pmid = 1907273 | issue = 22 }}
* {{cite journal | author = Johnson JL, Rajagopalan KV, Mukund S, Adams MW | year = 1993 | title = Identification of molybdopterin as the organic component of the tungsten cofactor in four enzymes from hyperthermophilic Archaea | journal = J. Biol. Chem.  | volume = 268 | pages = 4848&ndash;52  | pmid = 8444863 | issue = 7 }}
* {{cite journal | author = Roy R, Menon AL, Adams MW | year = 2001 | title = Aldehyde oxidoreductases from Pyrococcus furiosus | journal = Methods Enzymol.  | volume = 331 | pages = 132&ndash;44  | pmid = 11265456 | doi = 10.1016/S0076-6879(01)31052-2 }}
 
{{InterPro content|IPR013983}}
 
[[Category:EC 1.2.7]]
[[Category:Enzymes of unknown structure]]
 
 
{{1.2-enzyme-stub}}

Latest revision as of 07:42, 27 May 2014

Hello! My name is Porfirio. I smile that I could join to the entire globe. I live in Brazil, in the south region. I dream to visit the different nations, to look for familiarized with intriguing individuals.

Here is my web page; how can i make money fast