Inherent versatility of P-450 oxygenase. Conferring dehydroepiandrosterone hydroxylase activity to P-450 2a-4 by a single amino acid mutation at position 117.

This publication has 17 references indexed in Scilit:

• High-resolution crystal structure of cytochrome P450cam
  Published by Elsevier ,2005
• Crystal Structure of Hemoprotein Domain of P450BM-3, a Prototype for Microsomal P450's
  Science, 1993
• Engineering cytochrome P-450_cam to increase the stereospecificity and coupling of aliphatic hydroxylation
  Protein Engineering, Design and Selection, 1993
• Alteration of the substrate specificity of mouse 2A P450s by the identity of residue-209: Steroid-binding site and orientation
  The Journal of Steroid Biochemistry and Molecular Biology, 1992
• Mapping determinants of the substrate selectivities of P450 enzymes by site-directed mutagenesis
  Trends in Pharmacological Sciences, 1992
• Neurosteroid metabolism. 7α-Hydroxylation of dehydroepiandrosterone and pregnenolone by rat brain microsomes
  Biochemical Journal, 1992
• Cytochrome P450: cellular distribution and structural considerations
  Current Opinion in Structural Biology, 1992
• [2] Modeling of mammalian P450s on basis of P450cam x-ray structure
  Published by Elsevier ,1991
• Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue
  Nature, 1989
• A new force field for molecular mechanical simulation of nucleic acids and proteins
  Journal of the American Chemical Society, 1984