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Published on: July 11, 2012
Purification and characterization of NAD-specific 6-phosphogluconate dehydrogenase from Leuconostoc lactis SHO-54
Hitomi Ohara1, Roy A Russell, Kazuyuki Uchida
1Toyota Biotechnology and Afforestation Laboratory, 1099 Aza Marune, Oaza Kurozasa, Miyoshi-chou, Nishikamogun, Aichi 470-0201, Japan. hitomi_ohara@mail.toyota.co.jp
Abstract:
The 6-phosphogluconate dehydrogenase (EC 1.1.1.44) from Leuconostoc lactis SHO-54 was purified with an overall yield of 38% and a specific activity of 140.0 units/mg protein. The enzyme had a tetrameric structure and a molecular mass of 32.8 kDa. The amino acid composition of the purified enzyme was determined, and the enzyme contained no sulfhydryl amino acids. The K(m) values for 6-phosphogluconate and NAD were 0.95 mM and 0.32 mM, respectively.
