000 | 01934 a2200505 4500 | ||
---|---|---|---|
005 | 20250516234224.0 | ||
264 | 0 | _c20150622 | |
008 | 201506s 0 0 eng d | ||
022 | _a1422-0067 | ||
024 | 7 |
_a10.3390/ijms150916885 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aShao, Hua | |
245 | 0 | 0 |
_aBiochemical characterization of a carboxylesterase from the archaeon Pyrobaculum sp. 1860 and a rational explanation of its substrate specificity and thermostability. _h[electronic resource] |
260 |
_bInternational journal of molecular sciences _cSep 2014 |
||
300 |
_a16885-910 p. _bdigital |
||
500 | _aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't | ||
650 | 0 | 4 | _aAmino Acid Sequence |
650 | 0 | 4 |
_aArchaeal Proteins _xantagonists & inhibitors |
650 | 0 | 4 |
_aCarboxylic Ester Hydrolases _xantagonists & inhibitors |
650 | 0 | 4 |
_aCations _xpharmacology |
650 | 0 | 4 | _aCloning, Molecular |
650 | 0 | 4 |
_aEdetic Acid _xpharmacology |
650 | 0 | 4 |
_aEsters _xmetabolism |
650 | 0 | 4 | _aHot Temperature |
650 | 0 | 4 | _aHydrogen Bonding |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 | _aMolecular Docking Simulation |
650 | 0 | 4 | _aMolecular Dynamics Simulation |
650 | 0 | 4 | _aMolecular Sequence Data |
650 | 0 | 4 | _aMutagenesis, Site-Directed |
650 | 0 | 4 |
_aNitrophenols _xmetabolism |
650 | 0 | 4 | _aProtein Conformation |
650 | 0 | 4 | _aProtein Stability |
650 | 0 | 4 |
_aPyrobaculum _xenzymology |
650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
650 | 0 | 4 | _aSequence Alignment |
650 | 0 | 4 | _aSequence Homology, Amino Acid |
650 | 0 | 4 |
_aSolvents _xpharmacology |
650 | 0 | 4 | _aSubstrate Specificity |
650 | 0 | 4 |
_aTosyl Compounds _xpharmacology |
700 | 1 | _aXu, Li | |
700 | 1 | _aYan, Yunjun | |
773 | 0 |
_tInternational journal of molecular sciences _gvol. 15 _gno. 9 _gp. 16885-910 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.3390/ijms150916885 _zAvailable from publisher's website |
999 |
_c24217900 _d24217900 |