![Catalysts | Free Full-Text | Recent Advances in ω-Transaminase-Mediated Biocatalysis for the Enantioselective Synthesis of Chiral Amines Catalysts | Free Full-Text | Recent Advances in ω-Transaminase-Mediated Biocatalysis for the Enantioselective Synthesis of Chiral Amines](https://pub.mdpi-res.com/catalysts/catalysts-08-00254/article_deploy/html/images/catalysts-08-00254-g001.png?1570208485)
Catalysts | Free Full-Text | Recent Advances in ω-Transaminase-Mediated Biocatalysis for the Enantioselective Synthesis of Chiral Amines
![Fluorescence-based high-throughput screening system for R-ω-transaminase engineering and its substrate scope extension | SpringerLink Fluorescence-based high-throughput screening system for R-ω-transaminase engineering and its substrate scope extension | SpringerLink](https://media.springernature.com/lw685/springer-static/image/art%3A10.1007%2Fs00253-020-10444-y/MediaObjects/253_2020_10444_Sch1_HTML.png)
Fluorescence-based high-throughput screening system for R-ω-transaminase engineering and its substrate scope extension | SpringerLink
![PDF) Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17 PDF) Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17](https://i1.rgstatic.net/publication/326690866_Structural_dynamics_of_the_transaminase_active_site_revealed_by_the_crystal_structure_of_a_co-factor_free_omega-transaminase_from_Vibrio_fluvialis_JS17/links/5fb549eb4585154a5febd8a4/largepreview.png)
PDF) Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17
![Creation of (R)-Amine Transaminase Activity within an α-Amino Acid Transaminase Scaffold | ACS Chemical Biology Creation of (R)-Amine Transaminase Activity within an α-Amino Acid Transaminase Scaffold | ACS Chemical Biology](https://pubs.acs.org/cms/10.1021/acschembio.9b00888/asset/images/large/cb9b00888_0004.jpeg)
Creation of (R)-Amine Transaminase Activity within an α-Amino Acid Transaminase Scaffold | ACS Chemical Biology
![Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17 | Scientific Reports Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17 | Scientific Reports](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs41598-018-29846-0/MediaObjects/41598_2018_29846_Fig3_HTML.png)
Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17 | Scientific Reports
![Substrate profile of an ω-transaminase from Burkholderia vietnamiensis and its potential for the production of optically pure amines and unnatural amino acids - ScienceDirect Substrate profile of an ω-transaminase from Burkholderia vietnamiensis and its potential for the production of optically pure amines and unnatural amino acids - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S1381117713003421-fx1.jpg)
Substrate profile of an ω-transaminase from Burkholderia vietnamiensis and its potential for the production of optically pure amines and unnatural amino acids - ScienceDirect
![Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17 | Scientific Reports Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17 | Scientific Reports](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41598-018-29846-0/MediaObjects/41598_2018_29846_Fig1_HTML.png)
Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17 | Scientific Reports
![RCSB PDB - 4A6T: Crystal structure of the omega transaminase from Chromobacterium violaceum in complex with PLP RCSB PDB - 4A6T: Crystal structure of the omega transaminase from Chromobacterium violaceum in complex with PLP](https://cdn.rcsb.org/images/structures/4a6t_assembly-1.jpeg)
RCSB PDB - 4A6T: Crystal structure of the omega transaminase from Chromobacterium violaceum in complex with PLP
![PROCESS FOR THE IDENTIFICATION AND PREPARATION OF A (R)-SPECIFIC OMEGA- TRANSAMINASE - diagram, schematic, and image 44 PROCESS FOR THE IDENTIFICATION AND PREPARATION OF A (R)-SPECIFIC OMEGA- TRANSAMINASE - diagram, schematic, and image 44](https://www.patentsencyclopedia.com/img/20120156706_44.png)
PROCESS FOR THE IDENTIFICATION AND PREPARATION OF A (R)-SPECIFIC OMEGA- TRANSAMINASE - diagram, schematic, and image 44
![Catalysts | Free Full-Text | ω-Transaminase-Mediated Asymmetric Synthesis of (S)-1-(4-Trifluoromethylphenyl)Ethylamine Catalysts | Free Full-Text | ω-Transaminase-Mediated Asymmetric Synthesis of (S)-1-(4-Trifluoromethylphenyl)Ethylamine](https://www.mdpi.com/catalysts/catalysts-11-00307/article_deploy/html/images/catalysts-11-00307-sch001.png)
Catalysts | Free Full-Text | ω-Transaminase-Mediated Asymmetric Synthesis of (S)-1-(4-Trifluoromethylphenyl)Ethylamine
![Frontiers | Enhancing PLP-Binding Capacity of Class-III ω-Transaminase by Single Residue Substitution Frontiers | Enhancing PLP-Binding Capacity of Class-III ω-Transaminase by Single Residue Substitution](https://www.frontiersin.org/files/Articles/484947/fbioe-07-00282-HTML/image_m/fbioe-07-00282-g001.jpg)
Frontiers | Enhancing PLP-Binding Capacity of Class-III ω-Transaminase by Single Residue Substitution
![Mechanism‐Guided Computational Design of ω‐Transaminase by Reprograming of High‐Energy‐Barrier Steps - Yang - 2022 - Angewandte Chemie International Edition - Wiley Online Library Mechanism‐Guided Computational Design of ω‐Transaminase by Reprograming of High‐Energy‐Barrier Steps - Yang - 2022 - Angewandte Chemie International Edition - Wiley Online Library](https://onlinelibrary.wiley.com/cms/asset/d45abbff-2bb1-40a8-934b-cf5ee7c80501/anie202212555-toc-0001-m.jpg)
Mechanism‐Guided Computational Design of ω‐Transaminase by Reprograming of High‐Energy‐Barrier Steps - Yang - 2022 - Angewandte Chemie International Edition - Wiley Online Library
Computational Redesign of an ω-Transaminase from Pseudomonas jessenii for Asymmetric Synthesis of Enantiopure Bulky Amines | ACS Catalysis
![Structural studies reveal flexible roof of active site responsible for ω- transaminase CrmG overcoming by-product inhibition | Communications Biology Structural studies reveal flexible roof of active site responsible for ω- transaminase CrmG overcoming by-product inhibition | Communications Biology](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs42003-020-01184-w/MediaObjects/42003_2020_1184_Fig1_HTML.png)
Structural studies reveal flexible roof of active site responsible for ω- transaminase CrmG overcoming by-product inhibition | Communications Biology
![Redesign of (R)-Omega-Transaminase and Its Application for Synthesizing Amino Acids with Bulky Side Chain | SpringerLink Redesign of (R)-Omega-Transaminase and Its Application for Synthesizing Amino Acids with Bulky Side Chain | SpringerLink](https://media.springernature.com/lw685/springer-static/image/art%3A10.1007%2Fs12010-021-03616-7/MediaObjects/12010_2021_3616_Figa_HTML.png)
Redesign of (R)-Omega-Transaminase and Its Application for Synthesizing Amino Acids with Bulky Side Chain | SpringerLink
![PROCESS FOR THE IDENTIFICATION AND PREPARATION OF A (R)-SPECIFIC OMEGA- TRANSAMINASE - diagram, schematic, and image 46 PROCESS FOR THE IDENTIFICATION AND PREPARATION OF A (R)-SPECIFIC OMEGA- TRANSAMINASE - diagram, schematic, and image 46](https://www.patentsencyclopedia.com/img/20120156706_46.png)
PROCESS FOR THE IDENTIFICATION AND PREPARATION OF A (R)-SPECIFIC OMEGA- TRANSAMINASE - diagram, schematic, and image 46
![Evidence that glutamine transaminase and omega-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants - ScienceDirect Evidence that glutamine transaminase and omega-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0031942214001824-fx1.jpg)