tyrosine phenol lyase
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2022 ◽  
pp. 114547
Author(s):  
Hang-Qin Zhu ◽  
Wen-Ye Hu ◽  
Xiao-Ling Tang ◽  
Ren-Chao Zheng ◽  
Yu-Guo Zheng

2021 ◽  
Vol 7 ◽  
Author(s):  
Kil Koang Kwon ◽  
Haseong Kim ◽  
Soo-Jin Yeom ◽  
Eugene Rha ◽  
Jinju Lee ◽  
...  

Genetic circuits have been developed for quantitative measurement of enzyme activity, metabolic engineering of strain development, and dynamic regulation of microbial cells. A genetic circuit consists of several bio-elements, including enzymes and regulatory cassettes, that can generate the desired output signal, which is then used as a precise criterion for enzyme screening and engineering. Antagonists and inhibitors are small molecules with inhibitory effects on regulators and enzymes, respectively. In this study, an antagonist and an inhibitor were applied to a genetic circuit for a dynamic detection range. We developed a genetic circuit relying on regulators and enzymes, allowing for straightforward control of its output signal without additional genetic modification. We used para-nitrophenol and alanine as an antagonist of DmpR and inhibitor of tyrosine phenol-lyase, respectively. We show that the antagonist resets the detection range of the genetic circuit similarly to a resistor in an electrical logic circuit. These biological resistors in genetic circuits can be used as a rapid and precise controller of variable outputs with minimal circuit configuration.


Author(s):  
Shiming Tang ◽  
Yiwen Zheng ◽  
NanNan Zhao ◽  
Ying Lin ◽  
Shuangyan Han ◽  
...  

2020 ◽  
Vol 47 (8) ◽  
pp. 563-571
Author(s):  
Hongmei Han ◽  
Weizhu Zeng ◽  
Guoqiang Zhang ◽  
Jingwen Zhou

Abstract The formation of inclusion bodies (IBs) without enzyme activity in bacterial research is generally undesirable. Researchers have attempted to recovery the enzyme activities of IBs, which are commonly known as active IBs. Tyrosine phenol-lyase (TPL) is an important enzyme that can convert pyruvate and phenol into 3,4-dihydroxyphenyl-l-alanine (L-DOPA) and IBs of TPL can commonly occur. To induce the correct folding and recover the enzyme activity of the IBs, peptides, such as ELK16, DKL6, L6KD, ELP10, ELP20, L6K2, EAK16, 18A, and GFIL16, were fused to the carboxyl terminus of TPL. The results showed that aggregate particles of TPL-DKL6, TPL-ELP10, TPL-EAK16, TPL-18A, and TPL-GFIL16 improved the enzyme activity by 40.9%, 50.7%, 48.9%, 86.6%, and 97.9%, respectively. The peptides TPL-DKL6, TPL-EAK16, TPL-18A, and TPL-GFIL16 displayed significantly improved thermostability compared with TPL. L-DOPA titer of TPL-ELP10, TPL-EAK16, TPL-18A, and TPL-GFIL16, with cells reaching 37.8 g/L, 53.8 g/L, 37.5 g/L, and 29.1 g/L, had an improvement of 111%, 201%, 109%, and 63%, respectively. A higher activity and L-DOPA titer of the TPL-EAK16 could be valuable for its industrial application to biosynthesize L-DOPA.


2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Jubilee H. Munozvilla ◽  
Christian E. Loo ◽  
Jason P. Schwans

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