Dehydratase

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Thank you for visiting nature. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser or turn off compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. Complex polyketides of bacterial origin are biosynthesised by giant assembly-line like megaenzymes of the type 1 modular polyketide synthase PKS class.

Dehydratase

Dehydratases are a group of lyase enzymes that form double and triple bonds in a substrate through the removal of water. Dehydratases can act on hydroxyacyl-CoA with or without cofactors , and some have a metal and non-metal cluster act as their active site. 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. This enzyme -related article is a stub. You can help Wikipedia by expanding it. Contents move to sidebar hide. Article Talk. Read Edit View history. Tools Tools.

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Thank you for visiting nature. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser or turn off compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. The members of this family are involved in various biosynthetic and carbohydrate metabolic pathways. The active site is located at the monomer-monomer interface and contains residues from both the N-terminal recognition helix and the C-terminus of the dimeric counterpart.

Engineered polyketide synthases PKSs are promising synthetic biology platforms for the production of chemicals with diverse applications. Several crystal structures of DH domains have been solved, providing important structural insights into substrate selection and dehydration. The first DH domain, isolated from the third module in the borrelidin PKS, is specific towards a trans -cyclopentane-carboxylate-containing polyketide substrate. The second DH domain, isolated from the first module in the fluvirucin B 1 PKS, accepts an amide-containing polyketide intermediate. Sequence-structure analysis of these domains, in addition to previously published DH structures, display many significant similarities and key differences pertaining to substrate selection. Asha V. Nair, Alice Robson, … Paul R.

Dehydratase

Related to dehydratase: threonine dehydratase. All rights reserved. A subclass of lyases hydro-lyases that remove H and OH as H 2 O from a substrate, leaving a double bond, or add a group to a double bond by the elimination of water from two substances to form a third; synthase is sometimes used when the synthetic aspect of the reaction is emphasized. Some trivial names of enzymes in this subclass bear the generic term hydratase, emphasizing the reverse reaction. An enzyme that catalyzes the removal of oxygen and hydrogen from organic compounds in the form of water. Published by Houghton Mifflin Company.

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Figure 2. Publisher's note: Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations. ALAD2 carriers were potentially protected against adverse hemapoietic effects ZPP and hemoglobin levels , perhaps because of decreased lead bioavailability to heme pathway enzymes. In keeping with other CS family members, this mechanism is enabled through the polarization of the substrate thioester carbonyl by an active site oxyanion hole, resulting in formation of intermediate 6 Fig. Source Population Gene Variables Ziemsen et al. D X-ray crystal structure of a single PksI monomer. You can help Wikipedia by expanding it. To obtain the best experience, we recommend you use a more up to date browser or turn off compatibility mode in Internet Explorer. Weimberg, R. Close banner Close.

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Residues Ser and Thr from the C-terminal sequence motif participate in the formation of the substrate binding site Fig. Based on our available crystal structures both Lys80 and Lys were identified as potential candidates for this role in PksI. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. Smith et al. The cortical bone of the tibia represents a long-term storage depot with an elimination half-life for lead in excess of a decade. Kabsch, W. These data represent the first mechanistic description of a HCS cassette dehydratase, and establish a deviant catalytic mechanism in PksI, which diverges from that previously proposed in other HCS cassette decarboxylases To a stirred solution of 3,3-dimethylacrylic acid 0. Environ Res. PksI was amplified B. In the liganded structure, the active site is occupied by the substrate mimic glycerol, whose hydroxyl group can form a hydrogen bond with His Dihydroxyacid dehydratase is important for gametophyte development and disruption causes increased susceptibility to salinity stress in Arabidopsis. Ten studies reported data on lead levels in tibia bone and ALAD polymorphism as an outcome measure.