1.
Acta Crystallogr F Struct Biol Commun
; 71(Pt 8): 1012-6, 2015 Aug.
Artículo
en Inglés
| MEDLINE
| ID: mdl-26249691
RESUMEN
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 293â 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 P3121, with unit-cell parameters a = b = 104.68, c = 97.29â Å, and diffracted to 2.6â Å resolution. Structure determination is under way.