Engineering of cytochrome P450 2B1 specificity. Conversion of an androgen 16 beta-hydroxylase to a 15 alpha-hydroxylase.

This publication has 34 references indexed in Scilit:

• High-resolution crystal structure of cytochrome P450cam
  Published by Elsevier ,2005
• Mapping determinants of the substrate selectivities of P450 enzymes by site-directed mutagenesis
  Trends in Pharmacological Sciences, 1992
• Role of residue 478 as a determinant of the substrate specificity of cytochrome P450 2B1
  Biochemistry, 1992
• A hypervariable region of P450IIC5 confers progesterone 21-hydroxylase activity to P450IIC1
  Biochemistry, 1991
• A molecular model for the enzyme cytochrome P45017α, a major target for the chemotherapy of prostatic cancer
  Biochemical and Biophysical Research Communications, 1990
• 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
  Biochemical and Biophysical Research Communications, 1990
• Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue
  Nature, 1989
• Point mutations at threonine-301 modify substrate specificity of rabbit liver microsomal cytochromes P-450 (laurate (ω-1)-hydroxylase and testosterone 16α-hydroxylase)
  Biochemical and Biophysical Research Communications, 1989
• Evidence for functional and structural multiplicity of pregnenolone-16.alpha.-carbonitrile-inducible cytochrome P-450 isozymes in rat liver microsomes
  Biochemistry, 1987
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970