Article
Heterologous expression and characterization of wild-type human cytochrome P450 1A2 without conventional N-terminal modification in Escherichia coli.
Protein expression and purification - 1 Feb 2008
Kim Dong-Hyun, Kim Keon-Hee, Isin Emre M, Guengerich F Peter, Chae Ho Zoon, Ahn Taeho, Yun Chul-Ho
Abstract excerpt
In this study, wild-type human CYP1A2 without the conventional N-terminal modification (second codon GCT) or the truncation of the N-terminal hydrophobic region was functionally expressed in Escherichia coli. Its enzymatic properties were compared with N-terminally modified CYP1A2. Although modified CYP1A2 is almost all high-spin, some wild-type CYP1A2 shifted to low-spin. Spectral binding titrations with several...
Topics
- Amino Acid Sequence
- Base Sequence
- Codon
- Cytochrome P-450 CYP1A2
- Cytochrome P-450 CYP1A2 Inhibitors
- Deuterium
- Enzyme Inhibitors
- Escherichia coli
- Humans
- Hydrogen Peroxide
- Hydroxylation
- Kinetics
- Molecular Sequence Data