He, Y Q <br/><br/>
Interconversion of the androstenedione hydroxylase specificities of cytochromes P450 2B4 and 2B5 upon simultaneous site-directed mutagenesis of four key substrate recognition residues.  [electronic resource] 

 -  Archives of biochemistry and biophysics  Nov 1996 
 - 152-60 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0003-9861 
<br/><br/><label>Standard No.: </label>10.1006/abbi.1996.0493  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Androstenedione--metabolism<br/>Animals<br/>Aryl Hydrocarbon Hydroxylases<br/>Base Sequence<br/>Binding Sites<br/>Cloning, Molecular<br/>Cytochrome P-450 Enzyme System--chemistry<br/>Cytochrome P450 Family 2<br/>DNA Primers<br/>Escherichia coli<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Mutagenesis, Site-Directed<br/>Oxazines--metabolism<br/>Point Mutation<br/>Polymerase Chain Reaction<br/>Progesterone--metabolism<br/>Protein Conformation<br/>Rabbits<br/>Recombinant Proteins--chemistry<br/>Steroid 16-alpha-Hydroxylase<br/>Steroid Hydroxylases--chemistry<br/>Substrate Specificity