Site-directed mutagenesis and high-resolution NMR spectroscopy of the active site of porphobilinogen deaminase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00421a002
Reference24 articles.
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1. Crystal structures of hydroxymethylbilane synthase complexed with a substrate analog: a single substrate-binding site for four consecutive condensation steps;Biochemical Journal;2021-03-04
2. Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism;iScience;2021-03
3. Structural basis of pyrrole polymerization in human porphobilinogen deaminase;Biochimica et Biophysica Acta (BBA) - General Subjects;2018-09
4. Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of theBacillus megateriumenzyme at near-atomic resolution;Acta Crystallographica Section D Biological Crystallography;2014-02-15
5. Insights into the mechanism of pyrrole polymerization catalysed by porphobilinogen deaminase: high-resolution X-ray studies of theArabidopsis thalianaenzyme;Acta Crystallographica Section D Biological Crystallography;2013-02-16
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