The enzyme catalyses a step of the pentose phosphate pathway. The enzyme from the Gram-positive bacterium Leuconostoc mesenteroides prefers NADP+ while the enzyme from the Gram-negative bacterium Gluconacetobacter xylinus prefers NAD+. cf. EC 184.108.40.206, glucose-6-phosphate dehydrogenase (NADP+) and EC 220.127.116.118, glucose-6-phosphate dehydrogenase (NAD+).
Olive, C., Geroch, M.E. and Levy, H.R. Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetic studies. J. Biol. Chem.246 (1971) 2047–2057. [PMID: 4396688]
Lee, W.T. and Levy, H.R. Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction. Protein Sci.1 (1992) 329–334. [DOI] [PMID: 1304341]
Cosgrove, M.S., Naylor, C., Paludan, S., Adams, M.J. and Levy, H.R. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry37 (1998) 2759–2767. [DOI] [PMID: 9485426]
Ragunathan, S. and Levy, H.R. Purification and characterization of the NAD-preferring glucose 6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinum). Arch. Biochem. Biophys.310 (1994) 360–366. [DOI] [PMID: 8179320]