Glucose-6-phosphate dehydrogenase
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2008-07-08T01:40:28Z
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'''Glucose-6-phosphate dehydrogenase''' ('''G6PD''') is a cytosolic [[enzyme]] in the [[pentose phosphate pathway]] (see image), a [[metabolic pathway]] that supplies reducing energy to cells (such as [[erythrocyte]]s) by maintaining the level of the [[co-enzyme]] [[nicotinamide adenine dinucleotide|nicotinamide adenine dinucleotide phosphate]] (NADPH). The NADPH in turn maintains the level of [[glutathione]] in these cells that helps protect the red blood cells against [[oxidation|oxidative]] damage. Of greater quantitative importance is the production of NADPH for tissues actively engaged in biosynthesis of fatty acids and/or isoprenoids, such as the liver, mammary glands, adipose tissue, and the adrenal glands.
In higher plants, several isoforms of G6PDH have been reported, which are localized in the cytosol, the plastidic stroma, and peroxisomes. <ref>{{cite journal | first = | last = Corpas FJ et al. | title = A dehydrogenase-mediated recycling system of NADPH in plant peroxisomes | journal = Biochem. J.. | year = 1998 | volume = 330 | issue = 7 | pages = 777–784 | doi = }}</ref>
===Regulation===
'''Glucose-6-phosphate dehydrogenase''' is stimulated by its substrate NADP<sup>+</sup>. The usual ratio of NADPH/NADP<sup>+</sup> in the cytosol of tissues engaged in biosyntheses is about 100/1. Increased utilization of NADPH for fatty acid biosynthesis will dramatically increase the level of NADP<sup>+</sup>, thus stimulating '''G6PD''' to produce more NADPH.
G6PD converts [[glucose-6-phosphate]] into [[6-phosphoglucono-δ-lactone]] and is the rate-limiting enzyme of the ''pentose phosphate pathway''.
[[image:G6PD_mechanism.png|450px|center|Mechanism of G6PD]]
[[Glucose-6-phosphate dehydrogenase deficiency]] is very common worldwide, and cause [[acute hemolytic anemia]] in the presence of simple infection, ingestion of fava beans, or reaction with certain medicines, AAA, antibiotics, antipyretics, and antimalarials.
G6PD is remarkable for its genetic diversity. Many variants of G6PD, mostly produced from [[missense mutation]]s, have been described with wide ranging levels of [[enzyme activity]] and associated clinical symptoms. Two transcript variants encoding different [[isoform]]s have been found for this gene.<ref>{{cite web | title = Entrez Gene: G6PD glucose-6-phosphate dehydrogenase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2539| accessdate = }}</ref>
==See also==
* [[Glucose-6-phosphate dehydrogenase deficiency]]
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vulliamy T, Beutler E, Luzzatto L |title=Variants of glucose-6-phosphate dehydrogenase are due to missense mutations spread throughout the coding region of the gene. |journal=Hum. Mutat. |volume=2 |issue= 3 |pages= 159–67 |year= 1993 |pmid= 8364584 |doi= 10.1002/humu.1380020302 }}
*{{cite journal | author=Mason PJ |title=New insights into G6PD deficiency. |journal=Br. J. Haematol. |volume=94 |issue= 4 |pages= 585–91 |year= 1996 |pmid= 8826878 |doi= }}
*{{cite journal | author=Wajcman H, Galactéros F |title=[Glucose 6-phosphate dehydrogenase deficiency: a protection against malaria and a risk for hemolytic accidents] |journal=C. R. Biol. |volume=327 |issue= 8 |pages= 711–20 |year= 2004 |pmid= 15506519 |doi= }}
}}
{{refend}}
==References==
{{reflist|2}}
{{Enzyme references|EC_number=1.1.1.49|IUBMB_EC_number=1/1/1/49}}
==External links==
* [http://www.atsdr.cdc.gov/csem/nitrate/no3treatment_management.html#g6pd ATSDR - G6PD Deficiency]
{{Enzyme links|EC_number=1.1.1.49|IUBMB_EC_number=1/1/1/49}}
[[Category:EC 1.1.1]]
{{enzyme-stub}}
{{Alcohol oxidoreductases}}
{{Pentose phosphate pathway}}
[[de:Glucose-6-phosphat-Dehydrogenase]]
[[es:Glucosa-6-fosfato deshidrogenasa (G6FD)]]
[[fr:Glucose-6-phosphate déshydrogénase]]
[[hr:Glukoza-6-fosfat dehidrogenaza]]
[[it:Glucosio-6-fosfato deidrogenasi]]
[[ms:G6PD]]
[[pl:Dehydrogenaza glukozo-6-fosforanowa]]
[[zh:葡萄糖六磷酸鹽脫氫酶缺乏症]]
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