ArticleiScience2021
Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism.
Article in iScience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Assessing predictions on fitness effects of missense variants in HMBS in CAGI6.Human genetics · 2025Article
- FiTMuSiC: leveraging structural and (co)evolutionary data for protein fitness prediction.Human genomics · 2024Article
- Systematically testing human HMBS missense variants to reveal mechanism and pathogenic variation.American journal of human genetics · 2023Article
- Systematically testing human HMBS missense variants to reveal mechanism and pathogenic variation.bioRxiv : the preprint server for biology · 2023Article
- Characterisation of a common hotspot variant in acute intermittent porphyria sheds light on the mechanism of hydroxymethylbilane synthase function.FEBS open bio · 2022Article
- The crystal structures of the enzyme hydroxymethylbilane synthase, also known as porphobilinogen deaminase.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Combining X-rays, neutrons and electrons, and NMR, for precision and accuracy in structure-function studies.Acta crystallographica. Section A, Foundations and advances · 2021Article
- Acute Intermittent Porphyria: An Overview of Therapy Developments and Future Perspectives Focusing on Stabilisation of HMBS and Proteostasis Regulators.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porphobilinogen deaminase (PBGD), the third enzyme in the heme biosynthesis, catalyzes the sequential coupling of four porphobilinogen (PBG) molecules into a heme precursor. Mutations in PBGD are associated with acute intermittent porphyria (AIP), a rare metabolic disorder. We used Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) to demonstrate that wild-type PBGD and AIP-associated mutant R167W both existed as holoenzymes (E
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