Dehydratase Explained
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.
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:
Notes and References
- dehydratase. The Free Dictionary.
- "Evidence that f-hydroxyacyl-CoA dehydrase purified from rat liver microsomes is of peroxisomal origin". Biochem. J. 287.
- Web site: ENZYME: 4.2.1.-. enzyme.expasy.org. 2016-11-05.
- RESERVED, INSERM US14 -- ALL RIGHTS. "Orphanet: Dehydratase deficiency". www.orpha.net. Retrieved 2016-11-01.
- 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.