Crystallographic studies of aspartate racemase fromLactobacillus sakeiNBRC 15893
2015 ◽
Vol 71
(8)
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pp. 1012-1016
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Keyword(s):
Aspartate racemase catalyzes the interconversion between L-aspartate and D-aspartate and belongs to the PLP-independent racemases. The enzyme from the lactic acid bacteriumLactobacillus sakeiNBRC 15893, isolated fromkimoto, 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 groupP3121, with unit-cell parametersa=b= 104.68,c= 97.29 Å, and diffracted to 2.6 Å resolution. Structure determination is under way.
2012 ◽
Vol 68
(11)
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pp. 1351-1353
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2014 ◽
Vol 70
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pp. 1560-1562
2015 ◽
Vol 71
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pp. 171-174
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2015 ◽
Vol 71
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pp. 354-357
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1999 ◽
Vol 55
(11)
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pp. 1946-1948
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