Crystal Structure of Diaminopimelate Epimerase from Arabidopsis thaliana, an Amino Acid Racemase Critical for l-Lysine Biosynthesis

2009 ◽  
Vol 385 (2) ◽  
pp. 580-594 ◽  
Author(s):  
Bindu Pillai ◽  
Vijayalakshmi A. Moorthie ◽  
Marco J. van Belkum ◽  
Sandra L. Marcus ◽  
Maia M. Cherney ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana ◽  
Amino Acid ◽  
Lysine Biosynthesis ◽  
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.

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

scholarly journals Crystal structure of Aspergillus fumigatus AroH , an aromatic amino acid aminotransferase

2021 ◽  
Author(s):  
Sharon Spizzichino ◽  
Gioena Pampalone ◽  
Mirco Dindo ◽  
Agostino Bruno ◽  
Luigina Romani ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Aspergillus Fumigatus ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acid Aminotransferase

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

Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its β-tubulin binding characterization

FEBS Letters ◽  
2010 ◽  
Vol 584 (16) ◽  
pp. 3533-3539 ◽  
Author(s):  
Lu Lu ◽  
Jie Nan ◽  
Wei Mi ◽  
Lan-Fen Li ◽  
Chun-Hong Wei ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Arabidopsis Thaliana ◽  
Tubulin Binding ◽  
Β Tubulin

The amino acid permease AAP8 is important for early seed development in Arabidopsis thaliana

Planta ◽  
2007 ◽  
Vol 226 (4) ◽  
pp. 805-813 ◽  
Author(s):  
Roberto Schmidt ◽  
Harald Stransky ◽  
Wolfgang Koch
Keyword(s):  
Arabidopsis Thaliana ◽  
Amino Acid ◽  
Seed Development ◽  
Amino Acid Permease ◽  
Early Seed Development
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