Probing the active site loop motif of murine ferrochelatase by random mutagenesis.

Abstract excerpt

Ferrochelatase catalyzes the terminal step of the heme biosynthetic pathway by inserting ferrous iron into protoporphyrin IX. A conserved loop motif was shown to form part of the active site and contact the bound porphyrin by molecular dynamics calculations and structural analysis. We applied a random mutagenesis approach and steady-state kinetic analysis to assess the role of the loop motif in murine...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Ferrochelatase
• Share to Gene Library
• Share to Lipids