| 000 | 01716 a2200493 4500 | ||
|---|---|---|---|
| 005 | 20250514065337.0 | ||
| 264 | 0 | _c20030910 | |
| 008 | 200309s 0 0 eng d | ||
| 022 | _a0021-9258 | ||
| 024 | 7 |
_a10.1074/jbc.M303767200 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aNørager, Sofie | |
| 245 | 0 | 0 |
_aLactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function. _h[electronic resource] |
| 260 |
_bThe Journal of biological chemistry _cAug 2003 |
||
| 300 |
_a28812-22 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 |
_aBinding Sites _xgenetics |
| 650 | 0 | 4 | _aCrystallization |
| 650 | 0 | 4 | _aDihydroorotate Dehydrogenase |
| 650 | 0 | 4 | _aElectrochemistry |
| 650 | 0 | 4 | _aHydrogen Bonding |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 |
_aLactococcus lactis _xenzymology |
| 650 | 0 | 4 | _aMathematics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Structure |
| 650 | 0 | 4 | _aMutagenesis |
| 650 | 0 | 4 |
_aOrotic Acid _xmetabolism |
| 650 | 0 | 4 | _aOxidation-Reduction |
| 650 | 0 | 4 |
_aOxidoreductases _xchemistry |
| 650 | 0 | 4 | _aOxidoreductases Acting on CH-CH Group Donors |
| 650 | 0 | 4 | _aPolymerase Chain Reaction |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aSpectrophotometry |
| 650 | 0 | 4 | _aStructure-Activity Relationship |
| 700 | 1 | _aArent, Susan | |
| 700 | 1 | _aBjörnberg, Olof | |
| 700 | 1 | _aOttosen, Mette | |
| 700 | 1 | _aLo Leggio, Leila | |
| 700 | 1 | _aJensen, Kaj Frank | |
| 700 | 1 | _aLarsen, Sine | |
| 773 | 0 |
_tThe Journal of biological chemistry _gvol. 278 _gno. 31 _gp. 28812-22 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1074/jbc.M303767200 _zAvailable from publisher's website |
| 999 |
_c12521667 _d12521667 |
||