Preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-arabinose metabolism
نویسندگان
چکیده
L-2-Keto-3-deoxyarabonate (L-KDA) dehydratase is a novel member of the dihydrodipicolinate synthase (DHDPS)/N-acetylneuraminate lyase (NAL) protein family and catalyzes the hydration of L-KDA to alpha-ketoglutaric semialdehyde. L-KDA dehydratase was overexpressed, purified and crystallized at 291 K using the hanging-drop vapour-diffusion method. The crystal diffracts to 2.0 A resolution using synchrotron radiation and belongs to the trigonal space group P3(1)21 or its enantiomorph P3(2)21, with unit-cell parameters a = b = 78.91, c = 207.71 A.
منابع مشابه
Identification and Characterization of L - Arabonate Dehydratase , L - 2 - Keto - 3 - deoxyarabonate Dehydratase , and L - Arabinolactonase Involved in an Alternative Pathway of L - Arabinose Metabolism
From the Faculty of Engineering, Kyoto University, Kyotodaigaku-katsura, Saikyo-ku, Kyoto 615-8530, Japan, the Institute of Advanced Energy, Kyoto University, Gokasyo, Uji, Kyoto 611-0011, Japan, the Department of Biomolecular Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan, and CREST, JST (Japan Science and Technology Agency), Gokasyo, Uji, Kyoto 611-00...
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عنوان ژورنال:
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications
دوره 63 شماره
صفحات -
تاریخ انتشار 2007