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Crystallographic studies of aspartate racemase from Lactobacillus sakei NBRC 15893
Author(s) -
Fujii Tomomi,
Yamauchi Takae,
Ishiyama Makoto,
Gogami Yoshitaka,
Oikawa Tadao,
Hata Yasuo
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15010572
Subject(s) - lactobacillus sakei , enzyme , lactic acid , chemistry , crystallography , bacteria , stereochemistry , lactobacillus , biochemistry , biology , fermentation , genetics
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 293 K 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 P 3 1 21, with unit‐cell parameters a = b = 104.68, c = 97.29 Å, and diffracted to 2.6 Å resolution. Structure determination is under way.