CAS 61461-61-8 ω-Transaminase, Aspergillus fumigatus - Analytical Products / Alfa Chemistry

CAT	AP61461618-A
CAS	61461-61-8

Description	recombinant, expressed in E. coli, ≥0.20 U/mg
Size	10MG, 50MG
Storage Conditions	−20°C

Amination of ω-Functionalized Aliphatic Primary Alcohols by a Biocatalytic Oxidation-Transamination Cascade

Mathias Pickl, Michael Fuchs, Silvia M Glueck, Kurt Faber

ChemCatChem. 2015 Oct;7(19):3121-3124.

PMID: 26583050

Kinetic Analysis of R-Selective ω-Transaminases for Determination of Intrinsic Kinetic Parameters and Computational Modeling of Kinetic Resolution of Chiral Amine

Sang-Woo Han, Jong-Shik Shin

Appl Biochem Biotechnol. 2020 May;191(1):92-103.

PMID: 31997135

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Case Study

ω-Transaminases for the Synthesis of Non-Racemic α-Chiral Primary Amines

Koszelewski, Dominik, et al. Trends in biotechnology 28.6 (2010): 324-332.

Optically pure amines are highly valuable products or key intermediates for many bioactive compounds; however, there are few efficient methods to prepare them. ω-Transaminases (TAs) can be used for the kinetic resolution of racemic amines or the asymmetric synthesis of amines from the corresponding ketones.
Two strategies using ω-TAs can be employed to prepare enantiomerically enriched amines: (i) kinetic resolution starting from racemic (rac) amines (Figure a), or (ii) asymmetric synthesis starting from prochiral ketones (Figure b), corresponding to the forward and reverse transamination reactions, respectively. By using the same ω-TA in either kinetic resolution or asymmetric synthesis, amines with opposite absolute configurations can be obtained. For example, if the ω-TA produces the (S)-enantiomer in asymmetric synthesis, the (R)-enantiomer can be obtained through kinetic resolution.

Deracemization of Racemic Amines Using ω-Transaminase and Nickel-Based Nanocatalysts

Jv, X., Wang, R., Sun, J., Ma, L., Zhao, P., Liu, J., ... & Wang, B. (2022). ACS Catalysis, 12(24), 15600-15608.

Chiral amines are key components in the development of numerous bioactive compounds. In this study, we developed a simultaneous chemo-enzymatic cascade approach to achieve isomeric configuration inversion of racemic amine mixtures using ω-transaminase.
One isomer is subjected to transamination by ω-transaminase, producing a ketone byproduct and an additional chiral substance. Then, a specially designed compatible nickel-based nanocatalyst is employed to selectively reduce and aminate the ketone byproduct, converting it back into the racemic amine, while keeping the opposite enantiomer unchanged. Combining these two steps in a single reaction system allows for a complete isomeric configuration inversion. Moreover, the desired chiral amine and an additional chiral substance are formed. The process consumes NH₃ and generates H₂O as the only byproduct.

Fluorescence-Based Kinetic Assays for High-Throughput Discovery and Design of Stereoselective ω-Transaminases

Scheidt, Thomas, Henrik Land, et al. Advanced Synthesis & Catalysis 357, no. 8 (2015): 1721-1731.

ω-Transaminases are valuable enzymes that catalyze the biocatalytic reductive amination of prochiral ketones to produce chiral amines with (R) or (S) configuration, achieving high optical purity and 100% yield. A novel and versatile assay has been developed to quantify ω-transaminase activity by characterizing the kinetics and enantioselectivity of novel or engineered enzymes, based on the conversion of 1-(6-methoxynaphthalen-2-yl)alkylamines.
The associated release of the acetylnaphthone product can be monitored through its bright fluorescence at 450 nm, offering very high sensitivity and selectivity. This assay principle can be used to quantify ω-transaminase catalysis across a wide range of enzyme activities. Due to the simplicity of the method and the low substrate consumption in microtiter plate format, this assay appears to be suitable for high-capacity liquid screening in transaminase directed evolution optimization.
For assay substrates with structural variations, an efficient modular synthetic route was developed, including racemate resolution via lipase-catalyzed transesterification, to provide enantiomerically pure (R) and (S) amines. These are crucial for rapid enantioselective profiling of ω-transaminases.