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.[citation needed]

A dehydratase 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.[4]

Common dehydratases include:

Delta-aminolevulinic acid dehydratase is found in blood and is involved in the production of the heme group of globins.[5] People exposed to lead will have a decrease in ADA-D activity.[6]

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.[7]

Arogenate dehydratase is found mostly in the chloroplasts of higher plants. It catalyzes the reaction of turning L-arogenate into L-phenylalanine.[8]


  1. ^ "dehydratase". The Free Dictionary.
  2. ^ "Evidence that f-hydroxyacyl-CoA dehydrase purified from rat liver microsomes is of peroxisomal origin". Biochem. J. 287.
  3. ^ "ENZYME: 4.2.1.-". Retrieved 2016-11-05.
  4. ^ RESERVED, INSERM US14 -- ALL RIGHTS. "Orphanet: Dehydratase deficiency". Retrieved 2016-11-01.
  5. ^ Reference, Genetics Home. "ALAD gene". Genetics Home Reference. Retrieved 2016-11-04.
  6. ^ Burch; Siegel. "Improved Method for Measurement of delta-Aminolevulinic Acid DehydrataseActivity of Human Erythrocytes". Clinical Chemistry. 17.
  7. ^ 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.
  8. ^ Jung; Zamir; Jensen. "Chloroplasts of higher plants synthesize L-phenylalanine via L-arogenate". Proc. Nati. Acad. Sci. USA. 83.

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