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Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism.
Bustad, Helene J; Kallio, Juha P; Laitaoja, Mikko; Toska, Karen; Kursula, Inari; Martinez, Aurora; Jänis, Janne.
Affiliation
  • Bustad HJ; Department of Biomedicine, University of Bergen, Jonas Lies vei 91, 5009 Bergen, Norway.
  • Kallio JP; Department of Biomedicine, University of Bergen, Jonas Lies vei 91, 5009 Bergen, Norway.
  • Laitaoja M; Department of Chemistry, University of Eastern Finland, 80130 Joensuu, Finland.
  • Toska K; Norwegian Porphyria Centre (NAPOS), Department for Medical Biochemistry and Pharmacology, Haukeland University Hospital, 5021 Bergen, Norway.
  • Kursula I; Department of Biomedicine, University of Bergen, Jonas Lies vei 91, 5009 Bergen, Norway.
  • Martinez A; Faculty of Biochemistry and Molecular Medicine, University of Oulu, 90570 Oulu, Finland.
  • Jänis J; Department of Biomedicine, University of Bergen, Jonas Lies vei 91, 5009 Bergen, Norway.
iScience ; 24(3): 102152, 2021 Mar 19.
Article in En | MEDLINE | ID: mdl-33665570
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Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: IScience Year: 2021 Document type: Article Affiliation country: Country of publication:
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Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: IScience Year: 2021 Document type: Article Affiliation country: Country of publication: