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.