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Evaluating the article Dehydratase
- There are no citations in this article so there is no way of knowing whether or not the information is accurate or where it came from.
- The only thing the article provides besides a definition is that there are four kinds of dehydratases with a brief description of what they act on. It does not elaborate on where the dehydratases are found nor any structural differences.
- It also mentions a lot of jargon that could be linked to other wikipedia pages.
- There is no bias or view point taken with this article.
- It does not provide any reference to the discovery of this enzyme nor dates to put the information in perspective.
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Dehydratases are a group of lyase enzymes that form double and triple bonds in a substrate through the removal of water.[1] They can be found in many places including the mitochondria, peroxisome and cytosol.[2] There are more than 150 different dehydratase enzymes[3] that are classified into four groups. Dehydratases can act on hydroxyacyl-CoA with or without cofactors, and some have a metal and non-metal cluster act as their active site.[4]
A dehyratase deficiency in the body can lead to a less severe condition of hyperphenylalaninemia, which involves an over presence of phenylalanine in the blood. It is caused by a genetic recessive disorder in the autosomal DNA.[5]
Common dehydratases include:
Delta-aminolevulinic acid dehydratase is found in blood and is involved in the production of the heme group of globins.[6] People exposed to lead will have a decrease in ADA-D activity.[7]
Serine dehydratase is mostly found in the liver and catalyzes the reaction of turning serine into pyruvate and ammonia. In a diet of increased protein, the activity of serine dehydratase is increased.[8]
Arogenate dehydratase is found mostly in the chloroplasts of higher plants. It catalyzes the reaction of turning L-arogenate into L-phenylalanine. [9]
Refernces[edit]
- ^ "dehydratase". The Free Dictionary.
- ^ "Evidence that f-hydroxyacyl-CoA dehydrase purified from rat liver microsomes is of peroxisomal origin". Biochem. J. 287.
- ^ "ENZYME: 4.2.1.-". enzyme.expasy.org. Retrieved 2016-10-31.
- ^ Wu, Guoyao (March 28, 2014). Amino Acids, Biochemistry and Nutrition: Medicine, Nutrition. Cram101. ISBN 9781439861899.
- ^ RESERVED, INSERM US14 -- ALL RIGHTS. "Orphanet: Dehydratase deficiency". www.orpha.net. Retrieved 2016-11-01.
{{cite web}}: CS1 maint: numeric names: authors list (link) - ^ Reference, Genetics Home. "ALAD gene". Genetics Home Reference. Retrieved 2016-11-04.
- ^ Burch; Siegel. "Improved Method for Measurement of delta-Aminolevulinic Acid DehydrataseActivity of Human Erythrocytes". Clinical Chemistry. 17.
- ^ Mauron, Jean; Mottu, Françoise; Spohr, Georges (1973-01-01). "Reciprocal Induction and Repression of Serine Dehydratase and Phosphoglycerate Dehydrogenase by Proteins and Dietary-Essential Amino Acids in Rat Liver". European Journal of Biochemistry. 32 (2): 331–342. doi:10.1111/j.1432-1033.1973.tb02614.x. ISSN 1432-1033.
- ^ Jung; Zamir; Jensen. "Chloroplasts of higher plants synthesize L-phenylalanine via L-arogenate". Proc. Nati. Acad. Sci. USA. 83.
{{cite journal}}: CS1 maint: multiple names: authors list (link)