75531-11-2Relevant academic research and scientific papers
Fairly marked enantioselectivity for the hydrolysis of amino acid esters by chemically modified enzymes
Yano, Yoshihiro,Shimada, Kenji,Okai, Jiro,Goto, Koichi,Matsumoto, Yoko,Ueoka, Ryuichi
, p. 1314 - 1318 (2007/10/03)
The hydrolysis (deacylation) of enantiomeric substrates by the chemically modified enzymes decanoyl-α-chymotrypsin and decanoyl-trypsin was studied. Reaction activity for decanoyl-α-chymotrypsin was lower than that for the native enzyme, although intriguingly the enantioselectivity was markedly enhanced as compared with the native enzyme. In particular, the apparently complete enantioselective catalysis was attained for the hydrolytic cleavage of p-nitrophenyl N-dodecanoyl- D(L)-phenylalaninates. The enhancement of enantioselectivity, however, was not observed for decanoyl-trypsin. These results suggest that the chemically modified α-chymotrypsin by addition of hydrophobic groups has promoted enantioselectivity for the hydrolysis of hydrophobic esters.
Hybrid Liposomes Coupled to Steric Control with High Enantioselectivity
Goto, Koichi,Matsumoto, Yoko,Ueoka, Ryuichi
, p. 3342 - 3346 (2007/10/02)
With respect to the hydrolysis of enantiomeric substrates (p-nitrophenyl N-dodecanoyl-D(L)-phenylalaninate; C12-D(L)-Phe-PNP) by the tripeptide catalyst (N-(benzyloxycarbonyl)-L-phenylalanyl-L-histidyl-L-leucine; Z-PheHisLeu), a remarkably high enantioselectivity (kLa/obsd/kDa/obsd = 28) along with marked rate-enhancement of the hydrolytic cleavage of C12-D(L)-Phe-PNP was obtained with specific coaggregates of 32 mol percent L-α-dipalmitoylphosphatidylcholine (DPPC) and 68 mol percent α--ω-hydroxypoly(oxy-1,2-ethanediyl) (TritonX-100).The enantioselectivity was maximized at the phase transition temperature (Tc) in the 65 mol percent DPPC/35 mol percent TritonX-100 and 32 mol percent DPPC/68 mol percent TritonX-100 coaggregate systems.The hydrophobicity and fluidity of the coaggregates can apparently be changed around Tc on the basis of isokinetic temperature and fluorescence parameter studies.
Mechanism of Enantioselective Ester Cleavage by Histidine-Containing Dipeptides at a Micellar Interface
Cleij, Marco C.,Drenth, Wiendelt,Nolte, Roeland J. M.
, p. 3883 - 3891 (2007/10/02)
Chiral p-nitrophenyl esters derived from the amino acid phenylalanine are cleaved by histidine-containing dipeptides at a micellar interface.High enantioselectivities (up to kL/kD = 30.4 at 0 deg C) are observed.Both the substrates and the catalysts contain an alternating sequence of hydrophobic and hydrophilic groups.Due to the need for hydration of the hydrophilic groups, the hydrophobic groups cannot dissolve completely into the micellar hydrocarbon phase.The kinetic data suggest that the micellar interface is capable of discriminating between transition states that have different hydrophilic and hydrophobic properties.One of the diastereomeric transition states is characterized by a hydrogen bond between the amide CO group of the ester and an NH group of the histidine-containing dipeptide.Upon formation of this hydrogen bond these polar CO and NH groups lose their hydrophilicity which allows the transfer of the adjacent apolar groups to the micellar hydrocarbon phase.The other diastereomeric transition state cannot form this hydrogen bond and the hydrophobic groups remain hydrated.Consequently, the latter transition state is of higher energy.The kinetic data reveal that it is important to prevent steric hinderance between the reactants in order to allow the unhindered formation of the hydrogen bond.
Effect of Cholesterol on the Stereoselective Hydrolysis in Artificial Membrane Systems
Ueoka, Ryuichi,Matsumoto, Yoko
, p. 3774 - 3778 (2007/10/02)
The catalytic efficiency and enantioselectivity for the hydrolysis of p-nitrophenyl N-dodecanoyl-D(L)-phenylalaninate (2b) in the catalytic system of N-tetradecanoyl-L-histidyl-L-leucine (1b) and didodecyldimethylammonium bromide (3a) were enhanced by addition of cholesterol at an optimum temperature (25 deg C).Furthermore, it is suggested that the hydrophobic interaction between reactants in the bilayer membrane system (3a) might be reduced by adding cholesterol on the basis of isokinetic temperature.It is concluded from these results that the fluidity of the artificial bilayer matrix (3a) varies upon addition of cholesterol.
