346585-61-3Relevant articles and documents
Activity and specificity studies of the new thermostable esterase EstDZ2
Myrtollari, Kamela,Katsoulakis, Nikolaos,Zarafeta, Dimitra,Pavlidis, Ioannis V.,Skretas, Georgios,Smonou, Ioulia
, (2020/09/16)
In this paper, we study the activity and specificity of EstDZ2, a new thermostable carboxyl esterase of unknown function, which was isolated from a metagenome library from a Russian hot spring. The biocatalytic reaction employing EstDZ2 proved to be an efficient method for the hydrolysis of aryl p-, o- or m-substituted esters of butyric acid and esters of secondary alcohols. Docking studies revealed structural features of the enzyme that led to activity differences among the different substrates.
Chemoenzymatic synthesis of optically active Mugetanol isomers: use of lipases and oxidoreductases in fragrance chemistry
Vieira, Gizelle A.B.,Lemos, Telma L.G.,de Mattos, Marcos Carlos,de Oliveira, Maria da Conceicao F.,Melo, Vania M.M.,de Gonzalo, Gonzalo,Gotor-Fernandez, Vicente,Gotor, Vicente
experimental part, p. 214 - 219 (2009/06/20)
Straightforward synthetic strategies for the preparation of optically active Mugetanol isomers have been developed through different independent chemoenzymatic routes implying the use of either alcohol dehydrogenases in aqueous media or lipases in organic
How substrate solvation contributes to the enantioselectivity of subtilisin toward secondary alcohols
Savile, Christopher K.,Kazlauskas, Romas J.
, p. 12228 - 12229 (2007/10/03)
The current rule to predict the enantiopreference of subtilisin toward secondary alcohols is based on the size of the substituents at the stereocenter and implies that the active site contains two differently sized pockets for these substituents. Several experiments are inconsistent with the current rule. First, the X-ray structures of subtilisin show there is only one pocket (the S1- pocket) approximately the size of a phenyl group to bind secondary alcohols. Second, the rule often predicts the incorrect enantiomer for reactions in water. To resolve these contradictions, we refine the current rule to show that subtilisin binds only one substituent of a secondary alcohol and leaves the other in solvent. To test this refined empirical rule, we show that the enantioselectivity of a series of secondary alcohols in water varied linearly with the difference in hydrophobicity (log P/P0) of the substituents. This hydrophobicity difference accounts for the solvation of one substituent in water. Copyright
