2627-86-3Relevant articles and documents
Catalytic Behaviour of Optically Active Amino Alcohol-Borane Complex in the Enantioselective Reduction of Acetophenone Oxime O-Alkyl Ethers
Itsuno, Shinichi,Sakurai, Yoshiki,Ito, Koichi,Hirao, Akira,Nakahama, Seiichi
, p. 395 - 396 (1987)
In the presence of the optically active amino alcohol-borane complex, an oxime ether was reduced with various hydride reducing agents to give a chiral primary amine of high optical purity.Catalytic use of the chiral complex was also investigated.
A new procedure for the synthesis of optically active t-butylphenylphosphinothioic acid
Drabowicz, Jzef,Pokora-Sobczak, Patrycja,Zajc, Adrian,Wach-Panfilow, Paulina
, p. 674 - 677 (2014)
A new procedure for the synthesis of optically active t-butylophenylphosphinothioic acid as an enantiomerically pure dextrorotatory enantiomer having the absolute configuration (R), by a reaction of the racemate of secondary t-butylphenylphosphine oxide with elemental sulfur in the presence of a molar equivalent of the levorotatory enantiomer of enantiomerically pure (S)-α-phenylethylamine, is reported. It is obvious that with the use of the dextrorotatory enantiomer of α-phenylethylamine, the levorotatory enantiomer of this thioacid will be isolated.
Influence of Z,E-isomerism on the chiral-optical properties of amides
Dem'yanovich,Shishkina
, p. 807 - 811 (1996)
The study of the chiral-optical properties of N-acyl-(-)-1-methyl-1,2,3,4-tetrahydroisoquinolines and their acyclic analogs, the n-acyl-(-)-1-phenylethylamines, with the known ratio of Z- and E-isomers showed that the Z-isomers are characterized by the negative Cotton effect in the region of the absorption band of the amide chromophore. The observed Cotton effects of amides of phenylethy lamine, which are higher by comparison with those of amides of tetrahydroisoquinoline, are explained by the interaction of the amide and aromatic chromophores, which are in proximity in certain conformations, possible for acyclic conformationally free phenylethylamides. 1997 Plenum Publishing Corporation.
Engineering transaminase for stability enhancement and site-specific immobilization through multiple noncanonical amino acids incorporation
Deepankumar, Kanagavel,Nadarajan, Saravanan Prabhu,Mathew, Sam,Lee, Sun-Gu,Yoo, Tae Hyeon,Hong, Eun Young,Kim, Byung-Gee,Yun, Hyungdon
, p. 417 - 421 (2015)
In general, conventional enzyme engineering utilizes 20 canonical amino acids to alter and improve the functional properties of proteins such as stability, and activity. In this study, we utilized the noncanonical amino acid incorporation technique to enh
Tuneable 3D printed bioreactors for transaminations under continuous-flow
Peris, Edgar,Okafor, Obinna,Kulcinskaja, Evelina,Goodridge, Ruth,Luis, Santiago V.,Garcia-Verdugo, Eduardo,O'Reilly, Elaine,Sans, Victor
, p. 5345 - 5349 (2017)
A method to efficiently immobilize enzymes on 3D printed continuous-flow devices is presented. Application of these chemically modified devices enables rapid screening of immobilization mechanisms and reaction conditions, simple transfer of optimised conditions into tailored printed microfluidic reactors and development of continuous-flow biocatalytic processes. The bioreactors showed good activity (8-20.5 μmol h-1 mgenz-1) in the kinetic resolution of 1-methylbenzylamine, and very good stability (ca. 100 h under flow).
Chromobacterium violaceum ω-transaminase variant Trp60Cys shows increased specificity for (S)-1-phenylethylamine and 4′-substituted acetophenones, and follows Swain-Lupton parameterisation
Cassimjee, Karim Engelmark,Humble, Maria Svedendahl,Land, Henrik,Abedi, Vahak,Berglund, Per
, p. 5466 - 5470 (2012)
For biocatalytic production of pharmaceutically important chiral amines the ω-transaminase enzymes have proven useful. Engineering of these enzymes has to some extent been accomplished by rational design, but mostly by directed evolution. By use of a homology model a key point mutation in Chromobacterium violaceum ω-transaminase was found upon comparison with engineered variants from homologous enzymes. The variant Trp60Cys gave increased specificity for (S)-1-phenylethylamine (29-fold) and 4′-substituted acetophenones (～5-fold). To further study the effect of the mutation the reaction rates were Swain-Lupton parameterised. On comparison with the wild type, reactions of the variant showed increased resonance dependence; this observation together with changed pH optimum and cofactor dependence suggests an altered reaction mechanism.
Engineering the active site of the amine transaminase from vibrio fluvialis for the asymmetric synthesis of aryl-alkyl amines and amino alcohols
Nobili, Alberto,Steffen-Munsberg, Fabian,Kohls, Hannes,Trentin, Ivan,Schulzke, Carola,H?hne, Matthias,Bornscheuer, Uwe T.
, p. 757 - 760 (2015)
Although the amine transaminase from Vibrio fluvialis has often been applied as a catalyst for the biocatalytic preparation of various chiral primary amines, it is not suitable for the transamination of α-hydroxy ketones and aryl-alkyl ketones bearing an alkyl substituent larger than a methyl group. We addressed this problem through a systematic mutagenesis study of active site residues to expand its substrate scope towards two bulky ketones. We identified two mutants (F85L/V153A and Y150F/V153A) showing 30-fold increased activity in the conversion of (S)-phenylbutylamine and (R)-phenylglycinol, respectively. Notably, they facilitated asymmetric synthesis of these amines with excellent enantiomeric purities of 98 ee. Excavating the active site: The constrained active site of the amine-transaminase from Vibrio fluvialis was engineered in order to achieve the conversion of bulky ketones. This led to the discovery of mutants with a 30-fold increase in activity which enabled the asymmetric synthesis of (S)-phenylbutylamine and (R)-phenylglycinol
Towards a continuous dynamic kinetic resolution of 1-phenylethylamine using a membrane assisted, two vessel process
Roengpithya, Chayaporn,Patterson, Darrell A.,Livingston, Andrew G.,Taylor, Paul C.,Irwin, Jacob L.,Parrett, Mark R.
, p. 3462 - 3463 (2007)
A continuous process with two separated reaction vessels provides a solution to the problems surrounding the combination of two catalysts in dynamic kinetic resolution reactions by retaining the biocatalyst in a lower temperature vessel with a microfiltration membrane and allowing the racemisation to occur efficiently in a higher temperature vessel. The Royal Society of Chemistry.
'Easy-on, easy-off' resolution of chiral 1-phenylethylamine catalyzed by Candida antarctica lipase B
Torres-Gavilan,Escalante,Regla,Lopez-Munguia,Castillo
, p. 2621 - 2624 (2007)
An 'easy-on, easy-off' process for the effective resolution of (±)-1-phenylethylamine was designed using the lipase B of Candida antarctica. This two step lipase-catalyzed process for the resolution of a chiral arylalkylamine involves a high-conversion enantioselective condensation of (R)-(+)-1-phenylethylamine with capric acid (conversion 99%, 24 h), followed by the hydrolysis of the corresponding synthesized (R)-(+)-amide (conversion 98%, 48 h). As a result, this efficient enzymatic process yields both (R)- and (S)-enantiomers of 1-phenylethylamine in high enantiomeric purity.
CRYSTAL STRUCTURES OF THE DIASTEREOMERIC SALT PAIR OF THE PROSTAGLANDIN INTERMEDIATE 1R,2S(+)-cis-2-HYDROXYCYCLOPENT-4-ENYLACETIC ACID WITH S- and R-1-PHENYLETHYLAMINE
Czugler. Matyas,Csoeregh, Ingeborg,Kalman, Alajos,Faigl, Ferenc,Acs, Maria
, p. 157 - 170 (1989)
Crystal structures of an enantiomeric salt pair formed between 1R,2S-cis-2-hydroxycyclopent-4-enylacetic acid (S-HCA) and R(+)-1-phenylethylamine (R-PEA) and the corresponding S-PEA salt have been determined by X-ray crystallography.The S-HCA:R-PEA 1:1 salt (R-HCAPEA hereafter) is orthorhombic, P212121, with the unit-cell parameters a=5.806(1), b=9.261(1), c=27.624(2) Angstroem and R=0.056 for 1162 reflections at ambient temperature.The S-HCA:S-PEA 1:1 salt (S-HCAPEA) is also orthorhombic, P212121, with the unit-cell data a=6.034(2), b=11.840(7), c=20.198(11) Angstroem at 170 K, R=0.082 for 1196 data measured at low temperatures (170 K).The R-HCAPEA salt has its two components assembled into an elongated rod-like shape via two-dimensional hydrogen bonding between cations and anions thus forming a well-ordered crystal.In contrast, the cation and anion in the S-HCAPEA salt forms a more globular aggregate and displays orientation disorder in the five-membered ring part of the anion and maintains an essentially one-dimensional hydrogen-bond network, while the total number of hydrogen bonds between cationic and anionic species remains three in both crystals.
