Article
Probing the active site loop motif of murine ferrochelatase by random mutagenesis.
The Journal of biological chemistry - 7 May 2004
Shi Zhen, Ferreira Gloria C
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
- Amino Acid Motifs
- Amino Acid Sequence
- Animals
- Binding Sites
- Cell Membrane
- Conserved Sequence
- Escherichia coli
- Ferrochelatase
- Gene Library
- Genetic Complementation Test
- Genetic Vectors
- Kinetics
- Lipids
- Liposomes
- Mice
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis