| 000 | 01747 a2200469 4500 | ||
|---|---|---|---|
| 005 | 20250516003817.0 | ||
| 264 | 0 | _c20101216 | |
| 008 | 201012s 0 0 eng d | ||
| 022 | _a1089-8638 | ||
| 024 | 7 |
_a10.1016/j.jmb.2010.09.049 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aRichter, Nina | |
| 245 | 0 | 0 |
_aThe three-dimensional structure of AKR11B4, a glycerol dehydrogenase from Gluconobacter oxydans, reveals a tryptophan residue as an accelerator of reaction turnover. _h[electronic resource] |
| 260 |
_bJournal of molecular biology _cDec 2010 |
||
| 300 |
_a353-62 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aAmino Acid Substitution |
| 650 | 0 | 4 | _aApraxia, Ideomotor |
| 650 | 0 | 4 |
_aBacterial Proteins _xchemistry |
| 650 | 0 | 4 |
_aCatalytic Domain _xgenetics |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 |
_aGluconobacter oxydans _xenzymology |
| 650 | 0 | 4 | _aHydrophobic and Hydrophilic Interactions |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aMutagenesis, Site-Directed |
| 650 | 0 | 4 |
_aNADP _xmetabolism |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
| 650 | 0 | 4 | _aSequence Homology, Amino Acid |
| 650 | 0 | 4 | _aStatic Electricity |
| 650 | 0 | 4 | _aStructural Homology, Protein |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 650 | 0 | 4 |
_aSugar Alcohol Dehydrogenases _xchemistry |
| 650 | 0 | 4 |
_aTryptophan _xchemistry |
| 700 | 1 | _aBreicha, Klaus | |
| 700 | 1 | _aHummel, Werner | |
| 700 | 1 | _aNiefind, Karsten | |
| 773 | 0 |
_tJournal of molecular biology _gvol. 404 _gno. 3 _gp. 353-62 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1016/j.jmb.2010.09.049 _zAvailable from publisher's website |
| 999 |
_c20215772 _d20215772 |
||