000			02112 a2200589 4500
005			20250515181026.0
264		0	_c20090910
008			200909s 0 0 eng d
022			_a1096-0384
024	7		_a10.1016/j.abb.2009.06.005 _2doi
040			_aNLM _beng _cNLM
100	1		_aHawwa, Renda
245	0	0	_aStructural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus. _h[electronic resource]
260			_bArchives of biochemistry and biophysics _cAug 2009
300			_a109-20 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, N.I.H., Extramural
650	0	4	_aAmino Acid Sequence
650	0	4	_aBinding Sites
650	0	4	_aCarboxylic Ester Hydrolases _xmetabolism
650	0	4	_aCloning, Molecular
650	0	4	_aCrystallization
650	0	4	_aDimerization
650	0	4	_aEnzyme Stability
650	0	4	_aEscherichia coli _xgenetics
650	0	4	_aGenome, Bacterial
650	0	4	_aGeobacillus stearothermophilus _xenzymology
650	0	4	_aHydrogen Bonding
650	0	4	_aHydrolysis
650	0	4	_aHydrophobic and Hydrophilic Interactions
650	0	4	_aKinetics
650	0	4	_aModels, Chemical
650	0	4	_aModels, Molecular
650	0	4	_aMolecular Sequence Data
650	0	4	_aPhosphoric Triester Hydrolases _xchemistry
650	0	4	_aPlasmids _xgenetics
650	0	4	_aPromoter Regions, Genetic
650	0	4	_aProtein Binding
650	0	4	_aProtein Structure, Secondary
650	0	4	_aSequence Homology, Amino Acid
650	0	4	_aSolubility
650	0	4	_aSubstrate Specificity
650	0	4	_aTemperature
650	0	4	_aTime Factors
650	0	4	_aTransformation, Bacterial
650	0	4	_aX-Rays
700	1		_aAikens, John
700	1		_aTurner, Robert J
700	1		_aSantarsiero, Bernard D
700	1		_aMesecar, Andrew D
773	0		_tArchives of biochemistry and biophysics _gvol. 488 _gno. 2 _gp. 109-20
856	4	0	_uhttps://doi.org/10.1016/j.abb.2009.06.005 _zAvailable from publisher's website
999			_c19024520 _d19024520