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]

Serine dehydratase is an example of a dehydratase. It utilizes PLP as a cofactor.

Pathology

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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

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Common dehydratases include:

References

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  1. ^ "Dehydratase". The Free Dictionary.
  2. ^ Cook L, Nagi MN, Suneja SK, Hand AR, Cinti DL (October 1992). "Evidence that beta-hydroxyacyl-CoA dehydrase purified from rat liver microsomes is of peroxisomal origin". The Biochemical Journal. 287 ( Pt 1) (Pt 1): 91–100. doi:10.1042/bj2870091. PMC 1133128. PMID 1417796.
  3. ^ "ENZYME: 4.2.1.-". enzyme.expasy.org. Retrieved 2016-11-05.
  4. ^ "Dehydratase deficiency". Orphanet. Retrieved 2016-11-01.
  5. ^ "ALAD gene". Genetics Home Reference. U.S. National Library of Medicine. Retrieved 2016-11-04.
  6. ^ Burch HB, Siegel AL (October 1971). "Improved Method for Measurement of delta-Aminolevulinic Acid DehydrataseActivity of Human Erythrocytes". Clinical Chemistry. 17 (10): 1038–41. doi:10.1093/clinchem/17.10.1038. PMID 4328740.
  7. ^ Mauron J, Mottu F, Spohr G (January 1973). "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): 331–42. doi:10.1111/j.1432-1033.1973.tb02614.x. PMID 4347092.
  8. ^ Jung E, Zamir LO, Jensen RA (October 1986). "Chloroplasts of higher plants synthesize L-phenylalanine via L-arogenate". Proceedings of the National Academy of Sciences of the United States of America. 83 (19): 7231–5. Bibcode:1986PNAS...83.7231J. doi:10.1073/pnas.83.19.7231. PMC 386689. PMID 3463961.
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