000 | 01952 a2200577 4500 | ||
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005 | 20250517133734.0 | ||
264 | 0 | _c20171006 | |
008 | 201710s 0 0 eng d | ||
022 | _a1878-4186 | ||
024 | 7 |
_a10.1016/j.str.2016.12.007 _2doi |
|
040 |
_aNLM _beng _cNLM |
||
100 | 1 | _aLight, Samuel H | |
245 | 0 | 0 |
_aTransferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity. _h[electronic resource] |
260 |
_bStructure (London, England : 1993) _c02 2017 |
||
300 |
_a295-304 p. _bdigital |
||
500 | _aPublication Type: Journal Article | ||
650 | 0 | 4 |
_aActinomycetales _xenzymology |
650 | 0 | 4 | _aAmino Acid Motifs |
650 | 0 | 4 | _aBinding Sites |
650 | 0 | 4 | _aBiocatalysis |
650 | 0 | 4 | _aCarbohydrate Conformation |
650 | 0 | 4 | _aCloning, Molecular |
650 | 0 | 4 | _aCrystallography, X-Ray |
650 | 0 | 4 |
_aEscherichia coli _xgenetics |
650 | 0 | 4 | _aGene Expression |
650 | 0 | 4 |
_aGlucosidases _xchemistry |
650 | 0 | 4 |
_aGlycoside Hydrolases _xchemistry |
650 | 0 | 4 | _aGlycosylation |
650 | 0 | 4 | _aHydrolysis |
650 | 0 | 4 | _aHydrophobic and Hydrophilic Interactions |
650 | 0 | 4 | _aKinetics |
650 | 0 | 4 |
_aListeria monocytogenes _xenzymology |
650 | 0 | 4 | _aModels, Molecular |
650 | 0 | 4 |
_aOligosaccharides _xchemistry |
650 | 0 | 4 | _aProtein Binding |
650 | 0 | 4 | _aProtein Interaction Domains and Motifs |
650 | 0 | 4 | _aProtein Structure, Secondary |
650 | 0 | 4 |
_aRecombinant Proteins _xchemistry |
650 | 0 | 4 | _aSubstrate Specificity |
650 | 0 | 4 |
_aWater _xchemistry |
700 | 1 | _aCahoon, Laty A | |
700 | 1 | _aMahasenan, Kiran V | |
700 | 1 | _aLee, Mijoon | |
700 | 1 | _aBoggess, Bill | |
700 | 1 | _aHalavaty, Andrei S | |
700 | 1 | _aMobashery, Shahriar | |
700 | 1 | _aFreitag, Nancy E | |
700 | 1 | _aAnderson, Wayne F | |
773 | 0 |
_tStructure (London, England : 1993) _gvol. 25 _gno. 2 _gp. 295-304 |
|
856 | 4 | 0 |
_uhttps://doi.org/10.1016/j.str.2016.12.007 _zAvailable from publisher's website |
999 |
_c26786272 _d26786272 |