51183-44-9Relevant academic research and scientific papers
Mutation of cysteine-295 to alanine in secondary alcohol dehydrogenase from thermoanaerobacter ethanolicus affects the enantioselectivity and substrate specificity of ketone reductions
Heiss, Christian,Laivenieks, Maris,Zeikus,Phillips, Robert S.
, p. 1659 - 1666 (2007/10/03)
The mutation of Cys-295 to alanine in Thermoanaerobacter ethanolicus secondary alcohol dehycrogenase (SADH) was performed to give C295A SADH, on the basis of molecular modeling studies utilizing the X-ray crystal structure coordinates of the highly homologous T. brockii secondary alcohol dehydrogenase (YKF.PDB). This mutant SADH has activity for 2-propanol comparable to wild-type SADH. However, the C295A mutation was found to cause a significant shift of enantioselectivity toward the (S)-configuration in the reduction of some ethynylketones to the corresponding chiral propargyl alcohols. This result confirms our prediction that Cys-295 is part of a small alkyl group binding pocket whose size determines the binding orientation of ketone substrates, and, hence, the stereochemical configuration of the product alcohol. Furthermore, C295A SADH has much higher actifity towards t-butyl and some α-branched ketones than does wild-type SADH. The C295A mutation does not affect the thioester reductase activity of SADH. The broader substrate specificity and altered stereoselectivity for C295A SADH make it a potentially useful tool for asymmetric reductions. Copyright
Enantioselective esterification of 2-methylpentanoic acid catalised via immobilized lipases in chrysotile and microemulsion-based gels
De Jesus, Paulo Cesar,Da Silva, Pedro Luiz Ferreira,Joao, Jair Juarez,Da Graca Nascimento, Maria
, p. 2893 - 2901 (2007/10/03)
Immobilized lipases in chrysotile and microemulsion-based gel (MBG) or organogel were used in the resolution of racemic 2-methylpentanoic acid that is a valuable synthetic intermediate for the preparation of, among other compounds, a number of steriochemically pure insect pheromones.
Lipase catalyzed resolution of chiral acids or alcohols using mixed carboxylic-carbonic anhydrides
Guibe-Jampel, Eryka,Chalecki, Zbigniew,Bassir, Mohamed,Gelo-Pujic, Mirjana
, p. 4397 - 4402 (2007/10/03)
Mixed carboxylic-carbonic anhydrides are efficient irreversible acyl transfer reagents for lipase catalyzed esterification in organic media, and can be used for the resolution of chiral carboxylic acids or alcohols.
Lipase catalyzed resolution of chiral acids using their mixed carboxylic carbonic anhydrides
Guibe-Jampel, Eryka,Bassir, Mohamed
, p. 421 - 422 (2007/10/02)
Mixed carboxylic-carbonix anhydrides are efficient irreversible acyl transfer reagents for lipase-catalyzed esterification in organic media, and can be used for the resolution of chiral carboxylic acids.
Lipase-Catalyzed Enantioselective Esterification of 2-Methylalkanoic Acids
Engel, Karl-Heinz
, p. 165 - 168 (2007/10/02)
A preference for (S)-enantiomers has been observed in the course of the esterification of racemic 2-methylalkanoic acids catalyzed by lipase from Candida cylindracea in heptane.
