| 000 | 01899 a2200541 4500 | ||
|---|---|---|---|
| 005 | 20250515165246.0 | ||
| 264 | 0 | _c20091020 | |
| 008 | 200910s 0 0 eng d | ||
| 022 | _a1083-351X | ||
| 024 | 7 |
_a10.1074/jbc.M808392200 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aPodzelinska, Kateryna | |
| 245 | 0 | 0 |
_aStructure of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway for phosphonate degradation. _h[electronic resource] |
| 260 |
_bThe Journal of biological chemistry _cJun 2009 |
||
| 300 |
_a17216-17226 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 | _aAmino Acid Substitution |
| 650 | 0 | 4 | _aBase Sequence |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aCatalytic Domain |
| 650 | 0 | 4 | _aCrystallography, X-Ray |
| 650 | 0 | 4 |
_aDNA Primers _xgenetics |
| 650 | 0 | 4 | _aEnzyme Stability |
| 650 | 0 | 4 |
_aEscherichia coli _xenzymology |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 |
_aLyases _xchemistry |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 |
_aMultienzyme Complexes _xchemistry |
| 650 | 0 | 4 | _aMutagenesis, Site-Directed |
| 650 | 0 | 4 |
_aOrganophosphonates _xmetabolism |
| 650 | 0 | 4 |
_aPhosphoric Diester Hydrolases _xchemistry |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
| 650 | 0 | 4 | _aSequence Homology, Amino Acid |
| 650 | 0 | 4 | _aSubstrate Specificity |
| 650 | 0 | 4 |
_aZinc _xmetabolism |
| 700 | 1 | _aHe, Shu-Mei | |
| 700 | 1 | _aWathier, Matthew | |
| 700 | 1 | _aYakunin, Alexander | |
| 700 | 1 | _aProudfoot, Michael | |
| 700 | 1 | _aHove-Jensen, Bjarne | |
| 700 | 1 | _aZechel, David L | |
| 700 | 1 | _aJia, Zongchao | |
| 773 | 0 |
_tThe Journal of biological chemistry _gvol. 284 _gno. 25 _gp. 17216-17226 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1074/jbc.M808392200 _zAvailable from publisher's website |
| 999 |
_c18798845 _d18798845 |
||