ArticleThe Biochemical journal1996
Recombinant human phenylalanine hydroxylase is a substrate for the ubiquitin-conjugating enzyme system.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 36 citations in OpenAlex.
- Hyperphenylalaninemia and serotonin deficiency in Dnajc12-deficient mice.Communications biology · 2024Article
- E3 Ubiquitin Ligase APC/CInternational journal of molecular sciences · 2020Article
- Proteasome-mediated degradation of tyrosine hydroxylase triggered by its phosphorylation: a new question as to the intracellular location at which the degradation occurs.Journal of neural transmission (Vienna, Austria : 1996) · 2018Review
- Linking genotypes database with locus-specific database and genotype-phenotype correlation in phenylketonuria.European journal of human genetics : EJHG · 2015Article
- Post-translational modifications and the Warburg effect.Oncogene · 2014Review
- Predicted effects of missense mutations on native-state stability account for phenotypic outcome in phenylketonuria, a paradigm of misfolding diseases.American journal of human genetics · 2007Article
- Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Missense mutations in the phenylalanine hydroxylase gene (PAH) can cause accelerated proteolytic turnover of PAH enzyme: a mechanism underlying phenylketonuria.Journal of inherited metabolic disease · 1999Article
- Tyrosine hydroxylase and Parkinson's disease.Molecular neurobiology · 1998Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme. Little is known about the rates of synthesis and degradation of PAH in vivo. The enzyme has been reported to have a half-life of approx. 2 days in rat liver and 7-8 h in rat hepatoma cells, but the mechanism of its degradation is not known. In the present study it is shown that the tetrameric form of the recombinant wild-type human enzyme is a substrate for the ubiquitin-conjugating enzyme system in the cytosolic fraction of rat testis. Our findings support the conclusion that multi-/poly-ubiquitination of human PAH plays a key role in the turnover of this cytosolic liver enzyme and provides a mechanism for the increased turnover observed for a number of recombinant mutant forms of the enzyme related to the metabolic disorder phenylketonuria, when expressed in eukaryotic cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.