000 01873 a2200517 4500
005 20250512003409.0
264 0 _c19890403
008 198904s 0 0 eng d
022 _a0006-291X
024 7 _a10.1016/0006-291x(89)92780-0
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aImai, Y
245 0 0 _aPoint mutations at threonine-301 modify substrate specificity of rabbit liver microsomal cytochromes P-450 (laurate (omega-1)-hydroxylase and testosterone 16 alpha-hydroxylase).
_h[electronic resource]
260 _bBiochemical and biophysical research communications
_cFeb 1989
300 _a717-22 p.
_bdigital
500 _aPublication Type: Journal Article
650 0 4 _aAmino Acid Sequence
650 0 4 _aAnimals
650 0 4 _aAryl Hydrocarbon Hydroxylases
650 0 4 _aAsparagine
650 0 4 _aCytochrome P-450 CYP4A
650 0 4 _aCytochrome P-450 Enzyme System
_xgenetics
650 0 4 _aDNA
_xgenetics
650 0 4 _aDecanoic Acids
_xmetabolism
650 0 4 _aIsoleucine
650 0 4 _aLauric Acids
_xmetabolism
650 0 4 _aMicrosomes, Liver
_xenzymology
650 0 4 _aMixed Function Oxygenases
_xgenetics
650 0 4 _aMutation
650 0 4 _aProgesterone
_xmetabolism
650 0 4 _aRabbits
650 0 4 _aSaccharomyces cerevisiae
_xenzymology
650 0 4 _aSerine
650 0 4 _aSpectrophotometry
650 0 4 _aSteroid 16-alpha-Hydroxylase
650 0 4 _aSteroid Hydroxylases
_xgenetics
650 0 4 _aStructure-Activity Relationship
650 0 4 _aSubstrate Specificity
650 0 4 _aTestosterone
_xmetabolism
650 0 4 _aThreonine
650 0 4 _aTransformation, Genetic
650 0 4 _aValine
700 1 _aNakamura, M
773 0 _tBiochemical and biophysical research communications
_gvol. 158
_gno. 3
_gp. 717-22
856 4 0 _uhttps://doi.org/10.1016/0006-291x(89)92780-0
_zAvailable from publisher's website
999 _c2499243
_d2499243