2015年8月
Crystallographic studies of aspartate racemase from Lactobacillus sakei NBRC 15893
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
- ,
- ,
- ,
- ,
- ,
- 巻
- 71
- 号
- 開始ページ
- 1012
- 終了ページ
- 1016
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1107/S2053230X15010572
- 出版者・発行元
- INT UNION CRYSTALLOGRAPHY
Aspartate racemase catalyzes the interconversion between L-aspartate and D-aspartate and belongs to the PLP-independent racemases. The enzyme from the lactic acid bacterium Lactobacillus sakei NBRC 15893, isolated from kimoto, is considered to be involved in D-aspartate synthesis during the brewing process of Japanese sake at low temperatures. The enzyme was crystallized at 293K by the sitting-drop vapour-diffusion method using 25%(v/v) PEG MME 550, 5%(v/v) 2-propanol. The crystal belonged to space group P3(1)21, with unit-cell parameters a = b = 104.68, c = 97.29 angstrom, and diffracted to 2.6 angstrom resolution. Structure determination is under way.
- リンク情報
- ID情報
-
- DOI : 10.1107/S2053230X15010572
- ISSN : 2053-230X
- Web of Science ID : WOS:000359352700015