{"doi":"10.1371/journal.pone.0089690","title":"Molecular Cloning of a Novel Glucuronokinase/Putative Pyrophosphorylase from Zebrafish Acting in an UDP-Glucuronic Acid Salvage Pathway","abstract":null,"journal":"PLoS ONE","year":2014,"id":596602,"datarank":0.37273599746820013,"base_score":2.4849066497880004,"endowment":2.4849066497880004,"self_citation_contribution":0.37273599746820013,"citation_network_contribution":0.0,"self_endowment_contribution":0.37273599746820013,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":11,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1528000,"name":"Robert Behmüller","orcid":null,"position":1,"is_corresponding":false},{"id":1528002,"name":"Raimund Tenhaken","orcid":null,"position":2,"is_corresponding":false},{"id":1527996,"name":"Roman Gangl","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Molecular Cloning of a Novel Glucuronokinase/Putative Pyrophosphorylase from Zebrafish Acting in an UDP-Glucuronic Acid Salvage Pathway","abstract":"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 31 ± 8 µM and accepting ATP as the only phosphate donor (Km: 59 ± 9 µM). 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.","is_dataset_classified":null,"base_score":2.4849066497880004,"endowment":2.4849066497880004,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"24586965","pmcid":"PMC3938481","openalex_id":"https://openalex.org/W2034251761","authors":[],"funders":[{"funder_name":"Austrian Science Fund FWF","grant_id":"P 25339","title":"Sugar kinases for cell wall biosynthesis"}],"total_grants":1,"fwci":0.5627,"citation_percentile":0.62456573,"influential_citations":0,"citation_trend":[{"year":2014,"count":1},{"year":2015,"count":2},{"year":2016,"count":1},{"year":2018,"count":1},{"year":2020,"count":1},{"year":2022,"count":1},{"year":2024,"count":2},{"year":2025,"count":2}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0089690&type=printable","host_type":"journal"},{"url":"https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0089690&type=printable","host_type":"publisher"},{"url":"http://dx.plos.org/10.1371/journal.pone.0089690","host_type":"publisher"},{"url":"https://doi.org/10.1371/journal.pone.0089690","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/24586965","host_type":"repository"},{"url":"http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.778.7876","host_type":""},{"url":"https://doaj.org/article/10299e97da2e428d88e09666a65bc588","host_type":"repository"},{"url":"http://europepmc.org/articles/PMC3938481","host_type":"repository"},{"url":"https://figshare.com/articles/dataset/_Molecular_Cloning_of_a_Novel_Glucuronokinase_Putative_Pyrophosphorylase_from_Zebrafish_Acting_in_an_UDP_Glucuronic_Acid_Salvage_Pathway_/948503","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3938481","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC3938481","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC3938481?pdf=render","host_type":"Europe_PMC"},{"url":"http://dx.doi.org/10.1371/journal.pone.0089690","host_type":""},{"url":"https://dx.doi.org/10.1371/journal.pone.0089690","host_type":""},{"url":"https://resolver.obvsg.at/urn:nbn:at:at-ubs:3-3055","host_type":""},{"url":"https://eplus.uni-salzburg.at/id/1712070","host_type":""}],"fields_of_study":["Proteoglycans and glycosaminoglycans research","Glycosylation and Glycoproteins Research","Carbohydrate Chemistry and Synthesis","0301 basic medicine","0303 health sciences","03 medical and health sciences","Animals","Phosphotransferases (Alcohol Group Acceptor)","Uridine Diphosphate Glucose Dehydrogenase","Uridine Diphosphate Glucuronic Acid","Zebrafish","Zebrafish Proteins"],"mesh_terms":["Animals","Uridine Diphosphate Glucose Dehydrogenase","Uridine Diphosphate Glucuronic Acid","Zebrafish","Phosphotransferases (Alcohol Group Acceptor)","Zebrafish Proteins"],"keywords":["Glucuronic acid","Biochemistry","Nucleotide sugar","Phosphofructokinase 2","Zebrafish","Glucuronates","Chemistry","Enzyme","Biosynthesis","Biology","Gene","Polysaccharide","Recombinant proteins","Arabidopsis thaliana","Science","Q","R","Saccharomyces cerevisiae","Zebrafish Proteins","Uridine Diphosphate Glucose Dehydrogenase","Phosphotransferases (Alcohol Group Acceptor)","Cations","Uridine Diphosphate Glucuronic Acid","Enzyme assays","Medicine","Animals","High performance liquid chromatography","Research Article"],"sdg_mappings":[{"sdg_number":2,"sdg_label":"2. Zero hunger"},{"sdg_number":0,"sdg_label":"Life below water"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"gen"},{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-28T10:44:48.877398Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}