The crystal structures of the enzyme hydroxymethylbilane synthase, also known as porphobilinogen deaminase. [PDF]
Acta Crystallogr F Struct Biol Commun, 2021 Helliwell JR.
europepmc +1 more source
Purification of Porphobilinogen Deaminase and the Sequencing and Expression of thehemC Gene of Rhodobacter Capsulatus. [PDF]
, 1998 Rhodobacter capsulatus uses the common tetrapyrrole pathway to synthesize heme, bacteriochlorophyll, siroheme and vitamin B-12. As part of our studies on the regulation of this pathway, the product of the hemC gene, porphobilinogen deaminase was purified
Canada, Keith A
core +2 more sources
Cytosolic persistence of mouse brain CYP1A1 in chronic heme deficiency [PDF]
, 2017 Previous work has demonstrated that the function of extrahepatic cytochrome P450 CYP1A1 is dependent on the availability of heme. CYP1A1 is involved in the activation of polyaromatic hydrocarbons.
Hoffmann, Francine +3 more
core
Emerging Regulatory Role of Nrf2 in Iron, Heme, and Hemoglobin Metabolism in Physiology and Disease
Frontiers in Veterinary Science, 2018 Iron has played an important role in energy production since the beginning of life, as iron-catalyzed redox reactions are required for energy production.
Shuya Kasai +3 more
doaj +1 more source
Delivering efficient liver-directed AAV-mediated gene therapy. [PDF]
, 2017 Adeno-associated virus vectors (AAV) have become the leading technology for liver-directed gene therapy. After the pioneering trials using AAV2 and AAV8 to treat haemophilia B, D’Avola et al.
Alexander, IE +3 more
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Chiral Biomarkers and Microfossils in Carbonaceous Meteorites [PDF]
Homochirality of the biomolecules (D-sugars of DNA and RNA and L-amino acids of proteins) is a fundamental property of all life on Earth. Abiotic mechanisms yield racemic mixtures (D/L=1) of chiral molecules and after the death of an organism, the ...
Hoover, Richard B.
core +2 more sources
Purification of human erythrocyte porphobilinogen deaminase.
South African medical journal = Suid-Afrikaanse tydskrif vir geneeskunde, 1991 Human erythrocyte porphobilinogen deaminase was isolated using ammonium sulphate fractionation and heat treatment, Sephadex G-25 and G-100 chromatography, di-ethylamino-ethyl anion-exchange chromatography, chromatofocusing over a pH gradient of 7-4 and, finally, hydrophobic interaction chromatography on a phenyl-Sepharose column.
A V, Corrigall +2 more
openaire +1 more source
UEG Week 2025 Poster Presentations
United European Gastroenterology Journal, Volume 13, Issue S8, Page S803-S1476, October 2025.
wiley +1 more source
Optimizing cofactor availability for the production of recombinant heme peroxidase in Pichia pastoris [PDF]
, 2015 Capone, Simona +4 more
core +4 more sources