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Titel
Molecular cloning of a novel glucuronokinase/putative pyrophosphorylase from zebrafish acting in an UDP-glucuronic acid salvage pathway / Roman Gangl, Robert Behmüller, Raimund Tenhaken
VerfasserGangl, Roman ; Behmüller, Robert ; Tenhaken, Raimund In der Gemeinsamen Normdatei der DNB nachschlagen
Erschienen in
PLoS ONE, Lawrence, Kan., 2014, Jg. 9, S. 1-15
ErschienenPublic Library of Science, 2014
SpracheEnglisch
DokumenttypAufsatz in einer Zeitschrift
Schlagwörter (EN)Enzyme assays / Zebrafish / High performance liquid chromatography / Recombinant proteins / Saccharomyces cerevisiae / Arabidopsis thaliana / Biosynthesis / Cations
Projekt-/ReportnummerP25339
ISSN1932-6203
URNurn:nbn:at:at-ubs:3-3055 Persistent Identifier (URN)
DOI10.1371/journal.pone.0089690 
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Molecular cloning of a novel glucuronokinase/putative pyrophosphorylase from zebrafish acting in an UDP-glucuronic acid salvage pathway [0.97 mb]
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Zusammenfassung (Englisch)

In animals, the main precursor for glycosaminoglycan and furthermore proteoglycan biosynthesis, like hyaluronic acid, is UDP-glucuronic acid, which is synthesized via the nucleotide sugar oxidation pathway. Mutations in this pathway cause severe developmental defects (deficiency in the initiation of heart valve formation). In plants, UDP-glucuronic acid is synthesized via two independent pathways. Beside the nucleotide sugar oxidation pathway, a second minor route to UDP-glucuronic acid exist termed the myo-inositol oxygenation pathway. Within this myo-inositol is ring cleaved into glucuronic acid, which is subsequently converted to UDP-glucuronic acid by glucuronokinase and UDP-sugar pyrophosphorylase. Here we report on a similar, but bifunctional enzyme from zebrafish (Danio rerio) which has glucuronokinase/putative pyrophosphorylase activity. The enzyme can convert glucuronic acid into UDP-glucuronic acid, required for completion of the alternative pathway to UDP-glucuronic acid via myo-inositol and thus establishes a so far unknown second route to UDP-glucuronic acid in animals. Glucuronokinase from zebrafish is a member of the GHMP-kinase superfamily having unique substrate specificity for glucuronic acid with a Km of 318 M and accepting ATP as the only phosphate donor (Km: 599 M). UDP-glucuronic acid pyrophosphorylase from zebrafish has homology to bacterial nucleotidyltransferases and requires UTP as nucleosid diphosphate donor. Genes for bifunctional glucuronokinase and putative UDP-glucuronic acid pyrophosphorylase are conserved among some groups of lower animals, including fishes, frogs, tunicates, and polychaeta, but are absent from mammals. The existence of a second pathway for UDP-glucuronic acid biosynthesis in zebrafish likely explains some previous contradictory finding in jekyll/ugdh zebrafish developmental mutants, which showed residual glycosaminoglycans and proteoglycans in knockout mutants of UDP-glucose dehydrogenase.

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CC-BY-Lizenz (4.0)Creative Commons Namensnennung 4.0 International Lizenz