Imai, Y <br/><br/>
Point mutations at threonine-301 modify substrate specificity of rabbit liver microsomal cytochromes P-450 (laurate (omega-1)-hydroxylase and testosterone 16 alpha-hydroxylase).  [electronic resource] 

 -  Biochemical and biophysical research communications  Feb 1989 
 - 717-22 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0006-291X 
<br/><br/><label>Standard No.: </label>10.1016/0006-291x(89)92780-0  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Animals<br/>Aryl Hydrocarbon Hydroxylases<br/>Asparagine<br/>Cytochrome P-450 CYP4A<br/>Cytochrome P-450 Enzyme System--genetics<br/>DNA--genetics<br/>Decanoic Acids--metabolism<br/>Isoleucine<br/>Lauric Acids--metabolism<br/>Microsomes, Liver--enzymology<br/>Mixed Function Oxygenases--genetics<br/>Mutation<br/>Progesterone--metabolism<br/>Rabbits<br/>Saccharomyces cerevisiae--enzymology<br/>Serine<br/>Spectrophotometry<br/>Steroid 16-alpha-Hydroxylase<br/>Steroid Hydroxylases--genetics<br/>Structure-Activity Relationship<br/>Substrate Specificity<br/>Testosterone--metabolism<br/>Threonine<br/>Transformation, Genetic<br/>Valine