Purification and Characterization of Extremely Thermo-Stable Glutamate Dehydrogenase from a Hyperthermophilic Archaeon,Thermococcus Litoralis

Biocatalysis ◽  
1994 ◽  
Vol 11 (2) ◽  
pp. 117-129 ◽  
Author(s):  
Toshihisa Ohshima ◽  
Norikazu Nishida
Keyword(s):  
Glutamate Dehydrogenase ◽  
Purification And Characterization ◽  
Thermococcus Litoralis ◽  
Hyperthermophilic Archaeon

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.

Purification and characterization of two glutamate dehydrogenase isoenzymes from Brassica napus

1999 ◽  
Vol 37 (10) ◽  
pp. 731-739 ◽  
Author(s):  
Masami Watanabe ◽  
Toshihiko Hoshino ◽  
Atsushi Kikuchi ◽  
Yukio Watanabe
Keyword(s):  
Brassica Napus ◽  
Glutamate Dehydrogenase ◽  
Purification And Characterization

Purification and characterization of glutamate dehydrogenase from Halobacterium of the Dead Sea

Biochemistry ◽  
1978 ◽  
Vol 17 (19) ◽  
pp. 4004-4010 ◽  
Author(s):  
Wolfgang Leicht ◽  
Moshe M. Werber ◽  
Henryk Eisenberg
Keyword(s):  
Glutamate Dehydrogenase ◽  
Dead Sea ◽  
Purification And Characterization ◽  
The Dead
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