Efficient Conversion of Threonine to Allothreonine Using Immobilized Amino Acid Racemase and Temperature Cycles

2021 ◽  
Author(s):  
Kritsada Intaraboonrod ◽  
Andreas Seidel-Morgenstern ◽  
Heike Lorenz ◽  
Adrian E. Flood
Keyword(s):  
Amino Acid ◽  
Temperature Cycles ◽  
Efficient Conversion ◽  
Amino Acid Racemase

Characterization of a novel moderate-substrate specificity amino acid racemase from the hyperthermophilic archaeon Thermococcus litoralis

2021 ◽  
Author(s):  
Ryushi Kawakami ◽  
Chinatsu Kinoshita ◽  
Tomoki Kawase ◽  
Mikio Sato ◽  
Junji Hayashi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Enzyme Stability ◽  
Hyperthermophilic Archaea ◽  
Thermococcus Litoralis ◽  
Hyperthermophilic Archaeon ◽  
Aminobutyrate Aminotransferase ◽  
Chaperone Protein ◽  
Amino Acid Racemase

Abstract The amino acid sequence of the OCC_10945 gene product from the hyperthermophilic archaeon Thermococcus litoralis DSM5473, originally annotated as γ-aminobutyrate aminotransferase, is highly similar to that of the uncharacterized pyridoxal 5ʹ-phosphate (PLP)-dependent amino acid racemase from Pyrococcus horikoshii. The OCC_10945 enzyme was successfully overexpressed in Escherichia coli by co-expression with a chaperone protein. The purified enzyme demonstrated PLP-dependent amino acid racemase activity primarily toward Met and Leu. Although PLP contributed to enzyme stability, it only loosely bound to this enzyme. Enzyme activity was strongly inhibited by several metal ions, including Co2+ and Zn2+, and non-substrate amino acids such as l-Arg and l-Lys. These results suggest that the underlying PLP-binding and substrate recognition mechanisms in this enzyme are significantly different from those of the other archaeal and bacterial amino acid racemases. This is the first description of a novel PLP-dependent amino acid racemase with moderate substrate specificity in hyperthermophilic archaea.

Occurrence of a unique amino acid racemase in a basidiomycetous mushroom, Lentinus edodes

2003 ◽  
Vol 23 (2-6) ◽  
pp. 379-387 ◽  
Author(s):  
Akira Watanabe ◽  
Shiro Yamaguchi ◽  
Koichiro Urabe ◽  
Yasuhiko Asada
Keyword(s):  
Amino Acid ◽  
Lentinus Edodes ◽  
Basidiomycetous Mushroom ◽  
Unique Amino Acid ◽  
Amino Acid Racemase

scholarly journals Immobilization of an amino acid racemase for application in crystallization‐based chiral resolutions of asparagine monohydrate

2020 ◽  
Vol 20 (12) ◽  
pp. 550-561 ◽  
Author(s):  
Thiane Carneiro ◽  
Katarzyna Wrzosek ◽  
Katja Bettenbrock ◽  
Heike Lorenz ◽  
Andreas Seidel‐Morgenstern
Keyword(s):  
Amino Acid ◽  
Amino Acid Racemase ◽  
Asparagine Monohydrate

scholarly journals Discovery of a novel amino acid racemase through exploration of natural variation inArabidopsis thaliana

2015 ◽  
Vol 112 (37) ◽  
pp. 11726-11731 ◽  
Author(s):  
Renee C. Strauch ◽  
Elisabeth Svedin ◽  
Brian Dilkes ◽  
Clint Chapple ◽  
Xu Li
Keyword(s):  
Amino Acid ◽  
Functional Characterization ◽  
Chemical Diversity ◽  
Genome Wide Association ◽  
Specialized Metabolism ◽  
Catalytic Potential ◽  
Genome Wide ◽  
Important Challenge ◽  
Genetic Linkages ◽  
Amino Acid Racemase

Plants produce diverse low-molecular-weight compounds via specialized metabolism. Discovery of the pathways underlying production of these metabolites is an important challenge for harnessing the huge chemical diversity and catalytic potential in the plant kingdom for human uses, but this effort is often encumbered by the necessity to initially identify compounds of interest or purify a catalyst involved in their synthesis. As an alternative approach, we have performed untargeted metabolite profiling and genome-wide association analysis on 440 natural accessions ofArabidopsis thaliana. This approach allowed us to establish genetic linkages between metabolites and genes. Investigation of one of the metabolite–gene associations led to the identification ofN-malonyl-d-allo-isoleucine, and the discovery of a novel amino acid racemase involved in its biosynthesis. This finding provides, to our knowledge, the first functional characterization of a eukaryotic member of a large and widely conserved phenazine biosynthesis protein PhzF-like protein family. Unlike most of known eukaryotic amino acid racemases, the newly discovered enzyme does not require pyridoxal 5′-phosphate for its activity. This study thus identifies a newd-amino acid racemase gene family and advances our knowledge of plantd-amino acid metabolism that is currently largely unexplored. It also demonstrates that exploitation of natural metabolic variation by integrating metabolomics with genome-wide association is a powerful approach for functional genomics study of specialized metabolism.

Temperature Cycling Induced Deracemization of dl-Asparagine Monohydrate with Immobilized Amino Acid Racemase

2020 ◽  
Vol 21 (1) ◽  
pp. 306-313
Author(s):  
Kritsada Intaraboonrod ◽  
Isabel Harriehausen ◽  
Thiane Carneiro ◽  
Andreas Seidel-Morgenstern ◽  
Heike Lorenz ◽  
...  
Keyword(s):  
Amino Acid ◽  
Temperature Cycling ◽  
Amino Acid Racemase ◽  
Asparagine Monohydrate

Polarimetric Assay for the Medium-Throughput Determination of α-Amino Acid Racemase Activity

2004 ◽  
Vol 76 (4) ◽  
pp. 1184-1188 ◽  
Author(s):  
Dorian L. Schönfeld ◽  
Uwe T. Bornscheuer
Keyword(s):  
Amino Acid ◽  
Amino Acid Racemase
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