Replacing the carboxy-terminal 28 residues of rabbit liver P-450 (laurate (ω-1)-hydroxylase) with those of P-450 (testosterone 16α-hydroxylase) produces a new stereospecific hydroxylase activity

This publication has 13 references indexed in Scilit:

• Identification of Regions Functioning in Substrate Interaction of Rabbit Liver Cytochrome P-450 (Laurate (ω-1)-Hydroxylase)1
  The Journal of Biochemistry, 1989
• Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue
  Nature, 1989
• The importance of threonine‐301 from cytochromes P‐450 (laurate (ω‐1)‐hydroxylase and testosterone 16α‐hydroxylase) in substrate binding as demonstrated by site‐directed mutagenesis
  FEBS Letters, 1988
• Characterization of Rabbit Liver Cytochrome P-450 (Laurate ω-1 Hydroxylase) Synthesized in Transformed Yeast Cells1
  The Journal of Biochemistry, 1988
• Cytochrome P450: Molecular Architecture, Mechanism, and Prospects for Rational Inhibitor Design
  Pharmaceutical Research, 1988
• Cytochrome P-450 Related to P-4504 from Phenobarbital-Treated Rabbit Liver: Molecular Cloning of cDNA and Characterization of Cytochrome P-450 Obtained by Its Expression in Yeast Cells1
  The Journal of Biochemistry, 1987
• Expression inSaccharomyces cerevisiaeof Chimeric Cytochrome P450 cDNAs Constructed from cDNAs for Rat Cytochrome P450c and P450d
  DNA, 1987
• DNA sequencing with chain-terminating inhibitors
  Proceedings of the National Academy of Sciences, 1977