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ω-Transaminase from Ochrobactrum anthropi Is Devoid of Substrate and Product Inhibitions
Eul-Soo Park, Jong‐Shik Shin
Yonsei University
来源Applied and Environmental Microbiology
年份2013
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摘要 · 完整
ω-Transaminases display complicated inhibitions by ketone products and both enantiomers of amine substrates. Here, we report the first example of ω-transaminase devoid of such inhibitions. Owing to the lack of enzyme inhibitions, the ω-transaminase from Ochrobactrum anthropi enabled efficient kinetic resolution of α-methylbenzylamine (500 mM) even without product removal.
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学术脉络
学科主题
生物医学Enzyme Catalysis and Immobilization
Enzyme Structure and Function · Carbohydrate Chemistry and Synthesis
参考文献 24
Free energy analysis of ω-transaminase reactions to dissect how the enzyme controls the substrate selectivity
被引 32Eul-Soo Park, Jong‐Shik Shin · Enzyme and Microbial Technology · 2011
Features and technical applications of ω-transaminases
被引 202M. Shaheer Malik, Eul-Soo Park, Jong‐Shik Shin · Applied Microbiology and Biotechnology · 2012
Molecular determinants for substrate selectivity of ω-transaminases
被引 73Eul-Soo Park, Minji Kim, Jong‐Shik Shin · Applied Microbiology and Biotechnology · 2011
此处列出前 3 条
施引文献 32
Transaminase biocatalysis: optimization and application
被引 475Fei Guo, Per Berglund · Green Chemistry · 2016
Discovery, Engineering, and Synthetic Application of Transaminase Biocatalysts
被引 373Iustina Slabu, James L. Galman, Richard C. Lloyd · ACS Catalysis · 2017
Recent achievements in developing the biocatalytic toolbox for chiral amine synthesis
被引 251Hannes Kohls, Fabian Steffen‐Munsberg, Matthias Höhne · Current Opinion in Chemical Biology · 2014
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