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ダウンロード数 : ?
ID 116135
著者
Kinoshita, Chinatsu Tokushima University
Kawase, Tomoki Tokushima University
Sato, Mikio Tokushima University
櫻庭, 春彦 Kagawa University
キーワード
pyridoxal 5ʹ-phosphate
amino acid racemase
substrate specificity
Thermococcus litoralis
資料タイプ
学術雑誌論文
抄録
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.
掲載誌名
Bioscience, Biotechnology, and Biochemistry
ISSN
09168451
13476947
cat書誌ID
AA10824164
出版者
Japan Society for Bioscience, Biotechnology, and Agrochemistry|Oxford University Press
85
7
開始ページ
1650
終了ページ
1657
発行日
2021-05-04
備考
論文本文は2022-05-04以降公開予定
権利情報
This is a pre-copyedited, author-produced version of an article accepted for publication in Bioscience, Biotechnology, and Biochemistry following peer review. The version of record Volume 85, Issue 7, July 2021, Pages 1650–1657 is available online at: https://doi.org/10.1093/bbb/zbab078.
EDB ID
出版社版DOI
出版社版URL
言語
eng
著者版フラグ
その他
部局
生物資源系