Recent Advances in Enzyme Engineering through Incorporation of Unnatural Amino Acids

2019 ◽  
Vol 24 (4) ◽  
pp. 592-604 ◽  
Author(s):  
Yumi Won ◽  
Amol D. Pagar ◽  
Mahesh D. Patil ◽  
Philip E. Dawson ◽  
Hyungdon Yun
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Enzyme Engineering ◽  
Recent Advances

Recent advancements in enzyme engineering via site-specific incorporation of unnatural amino acids

2021 ◽  
Vol 37 (12) ◽  
Author(s):  
Hang-Qin Zhu ◽  
Xiao-Ling Tang ◽  
Ren-Chao Zheng ◽  
Yu-Guo Zheng
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Enzyme Engineering ◽  
Site Specific

Recent advances and concepts in substrate specificity determination of proteases using tailored libraries of fluorogenic substrates with unnatural amino acids

2015 ◽  
Vol 396 (4) ◽  
pp. 329-337 ◽  
Author(s):  
Wioletta Rut ◽  
Paulina Kasperkiewicz ◽  
Anna Byzia ◽  
Marcin Poreba ◽  
Katarzyna Groborz ◽  
...  
Keyword(s):  
Amino Acids ◽  
Substrate Specificity ◽  
Phage Display ◽  
Unnatural Amino Acids ◽  
Fluorogenic Substrates ◽  
Recent Advances ◽  
Positional Scanning ◽  
Binding Pockets ◽  
Natural Amino Acids

Abstract Substrate specificity of proteases can be determined using several methods among which the most frequently used are positional scanning library, proteomics and phage display. Classic approaches can deliver information about preferences for natural amino acids in binding pockets of virtually all proteases. However, recent studies demonstrate the ability to obtain much more information by application of unnatural amino acids to positional scanning library approaches. This knowledge can be used for the design of more active and specific substrates, inhibitors and activity based probes. In this minireview we describe recent strategies and concepts for the design and application of fluorogenic substrates library tailored for exopeptidases and endopeptidases.

scholarly journals Enzymatic aminoacylation of tRNA with unnatural amino acids

2006 ◽  
Vol 103 (12) ◽  
pp. 4356-4361 ◽  
Author(s):  
M. C. T. Hartman ◽  
K. Josephson ◽  
J. W. Szostak
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids

scholarly journals Transferability of N-terminal mutations of pyrrolysyl-tRNA synthetase in one species to that in another species on unnatural amino acid incorporation efficiency

Amino Acids ◽  
2020 ◽  
Author(s):  
Thomas L. Williams ◽  
Debra J. Iskandar ◽  
Alexander R. Nödling ◽  
Yurong Tan ◽  
Louis Y. P. Luk ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Genetic Code ◽  
Unnatural Amino Acids ◽  
Trna Synthetase ◽  
Unnatural Amino Acid ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Genetic Code Expansion ◽  
Incorporation Efficiency

AbstractGenetic code expansion is a powerful technique for site-specific incorporation of an unnatural amino acid into a protein of interest. This technique relies on an orthogonal aminoacyl-tRNA synthetase/tRNA pair and has enabled incorporation of over 100 different unnatural amino acids into ribosomally synthesized proteins in cells. Pyrrolysyl-tRNA synthetase (PylRS) and its cognate tRNA from Methanosarcina species are arguably the most widely used orthogonal pair. Here, we investigated whether beneficial effect in unnatural amino acid incorporation caused by N-terminal mutations in PylRS of one species is transferable to PylRS of another species. It was shown that conserved mutations on the N-terminal domain of MmPylRS improved the unnatural amino acid incorporation efficiency up to five folds. As MbPylRS shares high sequence identity to MmPylRS, and the two homologs are often used interchangeably, we examined incorporation of five unnatural amino acids by four MbPylRS variants at two temperatures. Our results indicate that the beneficial N-terminal mutations in MmPylRS did not improve unnatural amino acid incorporation efficiency by MbPylRS. Knowledge from this work contributes to our understanding of PylRS homologs which are needed to improve the technique of genetic code expansion in the future.

scholarly journals Recent Advances in Rapid Synthesis of Non-proteinogenic Amino Acids from Proteinogenic Amino Acids Derivatives via Direct Photo-Mediated C–H Functionalization

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5270
Author(s):  
Zhenbo Yuan ◽  
Xuanzhong Liu ◽  
Changmei Liu ◽  
Yan Zhang ◽  
Yijian Rao
Keyword(s):  
Amino Acids ◽  
Direct Synthesis ◽  
Environmentally Friendly ◽  
Powerful Method ◽  
Rapid Synthesis ◽  
Conservation Of Energy ◽  
Mild Conditions ◽  
Recent Advances ◽  
Recent Developments

Non-proteinogenic amino acids have attracted tremendous interest for their essential applications in the realm of biology and chemistry. Recently, rising C–H functionalization has been considered an alternative powerful method for the direct synthesis of non-proteinogenic amino acids. Meanwhile, photochemistry has become popular for its predominant advantages of mild conditions and conservation of energy. Therefore, C–H functionalization and photochemistry have been merged to synthesize diverse non-proteinogenic amino acids in a mild and environmentally friendly way. In this review, the recent developments in the photo-mediated C–H functionalization of proteinogenic amino acids derivatives for the rapid synthesis of versatile non-proteinogenic amino acids are presented. Moreover, postulated mechanisms are also described wherever needed.

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