| 000 | 01832 a2200493 4500 | ||
|---|---|---|---|
| 005 | 20250513104146.0 | ||
| 264 | 0 | _c19961224 | |
| 008 | 199612s 0 0 eng d | ||
| 022 | _a0003-9861 | ||
| 024 | 7 |
_a10.1006/abbi.1996.0493 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aHe, Y Q | |
| 245 | 0 | 0 |
_aInterconversion of the androstenedione hydroxylase specificities of cytochromes P450 2B4 and 2B5 upon simultaneous site-directed mutagenesis of four key substrate recognition residues. _h[electronic resource] |
| 260 |
_bArchives of biochemistry and biophysics _cNov 1996 |
||
| 300 |
_a152-60 p. _bdigital |
||
| 500 | _aPublication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S. | ||
| 650 | 0 | 4 |
_aAndrostenedione _xmetabolism |
| 650 | 0 | 4 | _aAnimals |
| 650 | 0 | 4 | _aAryl Hydrocarbon Hydroxylases |
| 650 | 0 | 4 | _aBase Sequence |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aCloning, Molecular |
| 650 | 0 | 4 |
_aCytochrome P-450 Enzyme System _xchemistry |
| 650 | 0 | 4 | _aCytochrome P450 Family 2 |
| 650 | 0 | 4 | _aDNA Primers |
| 650 | 0 | 4 | _aEscherichia coli |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aMutagenesis, Site-Directed |
| 650 | 0 | 4 |
_aOxazines _xmetabolism |
| 650 | 0 | 4 | _aPoint Mutation |
| 650 | 0 | 4 | _aPolymerase Chain Reaction |
| 650 | 0 | 4 |
_aProgesterone _xmetabolism |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aRabbits |
| 650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
| 650 | 0 | 4 | _aSteroid 16-alpha-Hydroxylase |
| 650 | 0 | 4 |
_aSteroid Hydroxylases _xchemistry |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 700 | 1 | _aSzklarz, G D | |
| 700 | 1 | _aHalpert, J R | |
| 773 | 0 |
_tArchives of biochemistry and biophysics _gvol. 335 _gno. 1 _gp. 152-60 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1006/abbi.1996.0493 _zAvailable from publisher's website |
| 999 |
_c8907324 _d8907324 |
||