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]}

Pathology

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]

Examples

Common dehydratases include:

• Delta-aminolevulinic acid dehydratase (ADA-D) 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]

References

External links

• Dehydratases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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