Abstract
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. © 2013, American Society for Microbiology.
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CITATION STYLE
Park, E. S., & Shin, J. S. (2013). ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions. Applied and Environmental Microbiology, 79(13), 4141–4144. https://doi.org/10.1128/AEM.03811-12
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