title: Purification and characterization of NAD-specific 6-phosphogluconate dehydrogenase from Leuconostoc lactis SHO-54.
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.
authors.affiliation: Toyota Biotechnology and Afforestation Laboratory, 1099 Aza Marune, Oaza Kurozasa, Miyoshi-chou, Nishikamogun, Aichi 470-0201, Japan. hitomi_ohara@mail.toyota.co.jp
authors.forename: Hitomi
authors.initials: H
authors.lastname: Ohara
authors.forename: Roy A
authors.initials: RA
authors.lastname: Russell
authors.forename: Kazuyuki
authors.initials: K
authors.lastname: Uchida
authors.forename: Hitoshi
authors.initials: H
authors.lastname: Kondo