Dehydratase
Today, Dehydratase is a topic of great relevance and interest to a wide audience. Over time, Dehydratase has acquired significant importance in different areas of society, from politics and economics to culture and everyday life. Its impact has been felt both locally and internationally, generating ongoing debates, controversies and investigations. In this article, we will explore the various facets of Dehydratase and analyze its influence in different contexts. From its origins to its current evolution, Dehydratase has proven to be a topic of great relevance and promises to continue being the subject of discussion and analysis in the future.
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
- ^ "Dehydratase". The Free Dictionary.
- ^ 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.
- ^ "ENZYME: 4.2.1.-". enzyme.expasy.org. Retrieved 2016-11-05.
- ^ "Dehydratase deficiency". Orphanet. Retrieved 2016-11-01.
- ^ "ALAD gene". Genetics Home Reference. U.S. National Library of Medicine. Retrieved 2016-11-04.
- ^ 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.
- ^ 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.
- ^ 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.
External links
- Dehydratases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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