Biocatalytic Access to Chiral Polyesters by an Artificial Enzyme Cascade Synthesis

ChemCatChem ◽  
2015 ◽  
Vol 7 (23) ◽  
pp. 3951-3955 ◽  
Author(s):  
Sandy Schmidt ◽  
Hanna C. Büchsenschütz ◽  
Christian Scherkus ◽  
Andreas Liese ◽  
Harald Gröger ◽  
...  
2019 ◽  
Vol 41 (4-5) ◽  
pp. 605-611 ◽  
Author(s):  
Takenori Satomura ◽  
Kousaku Horinaga ◽  
Shino Tanaka ◽  
Eiichiro Takamura ◽  
Hiroaki Sakamoto ◽  
...  

2015 ◽  
Vol 71 (12) ◽  
pp. 1475-1480
Author(s):  
Iuliia Iermak ◽  
Oksana Degtjarik ◽  
Fabian Steffler ◽  
Volker Sieber ◽  
Ivana Kuta Smatanova

The glyceraldehyde dehydrogenase fromThermoplasma acidophilum(TaAlDH) is a microbial enzyme that catalyzes the oxidation of D-glyceraldehyde to D-glycerate in the artificial enzyme cascade designed for the conversion of glucose to the organic solvents isobutanol and ethanol. Various mutants ofTaAlDH were constructed by a random approach followed by site-directed and saturation mutagenesis in order to improve the properties of the enzyme that are essential for its functioning within the cascade. Two enzyme variants, wild-typeTaAlDH (TaAlDHwt) and an F34M+S405N variant (TaAlDH F34M+S405N), were successfully crystallized. Crystals ofTaAlDHwt belonged to the monoclinic space groupP1211 with eight molecules per asymmetric unit and diffracted to a resolution of 1.95 Å.TaAlDH F34M+S405N crystallized in two different space groups: triclinicP1 with 16 molecules per asymmetric unit and monoclinicC121 with four molecules per asymmetric unit. These crystals diffracted to resolutions of 2.14 and 2.10 Å for theP1 andC121 crystals, respectively.


Talanta ◽  
2020 ◽  
Vol 220 ◽  
pp. 121374 ◽  
Author(s):  
Min Liu ◽  
Junsong Mou ◽  
Xiaohan Xu ◽  
Feifei Zhang ◽  
Jianfei Xia ◽  
...  

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Benedict Ryan Lukito ◽  
Zilong Wang ◽  
Balaji Sundara Sekar ◽  
Zhi Li

Abstract(R)-mandelic acid is an industrially important chemical, especially used for producing antibiotics. Its chemical synthesis often uses highly toxic cyanide to produce its racemic form, followed by kinetic resolution with 50% maximum yield. Here we report a green and sustainable biocatalytic method for producing (R)-mandelic acid from easily available styrene, biobased L-phenylalanine, and renewable feedstocks such as glycerol and glucose, respectively. An epoxidation-hydrolysis-double oxidation artificial enzyme cascade was developed to produce (R)-mandelic acid at 1.52 g/L from styrene with > 99% ee. Incorporation of deamination and decarboxylation into the above cascade enables direct conversion of L-phenylalanine to (R)-mandelic acid at 913 mg/L and > 99% ee. Expressing the five-enzyme cascade in an L-phenylalanine-overproducing E. coli NST74 strain led to the direct synthesis of (R)-mandelic acid from glycerol or glucose, affording 228 or 152 mg/L product via fermentation. Moreover, coupling of E. coli cells expressing L-phenylalanine biosynthesis pathway with E. coli cells expressing the artificial enzyme cascade enabled the production of 760 or 455 mg/L (R)-mandelic acid from glycerol or glucose. These simple, safe, and green methods show great potential in producing (R)-mandelic acid from renewable feedstocks.


2014 ◽  
Vol 31 ◽  
pp. S75
Author(s):  
Wolfgang Kroutil ◽  
Johann Sattler ◽  
Michael Fuchs ◽  
Verena Resch ◽  
Joerg Schrittwieser

The Analyst ◽  
2021 ◽  
Author(s):  
Huiying Xu ◽  
Lu Zheng ◽  
Yu Zhou ◽  
Bang-Ce Ye

Tumor-related exosomes, which are heterogeneous membrane-enclosed nanovesicles shed from cancer cells, have been widely recognized as potential noninvasive biomarkers for early cancer diagnosis. Herein, an artificial enzyme cascade amplification strategy...


2018 ◽  
Author(s):  
Fei He ◽  
Li Mi ◽  
Yanfei Shen ◽  
Toshiyuki Mori ◽  
Songqin Liu ◽  
...  

Developing highly efficient artificial enzymes that directly employ O<sub>2</sub> as terminal oxidant has long been pursued but has rarely achieved yet. We report Fe-N-C has unusual enzyme-like activity in both dehydrogenation and monoxygenation of organic substrates with ~100% selectivity by direct using O<sub>2</sub>.


2021 ◽  
Vol 11 (11) ◽  
pp. 4877
Author(s):  
Ravneet Mandair ◽  
Pinar Karagoz ◽  
Roslyn M. Bill

A triple mutant of NADP(H)-dependent malate dehydrogenase from thermotolerant Thermococcus kodakarensis has an altered cofactor preference for NAD+, as well as improved malate production compared to wildtype malate dehydrogenase. By combining mutant malate dehydrogenase with glucose dehydrogenase from Sulfolobus solfataricus and NAD+/NADH in a closed reaction environment, gluconate and malate could be produced from pyruvate and glucose. After 3 h, the yield of malate was 15.96 mM. These data demonstrate the feasibility of a closed system capable of cofactor regeneration in the production of platform chemicals.


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