Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism.
Adams, M.J., Ellis, G.H., Gover, S., Naylor, C.E., Phillips, C.(1994) Structure 2: 651-668
- PubMed: 7922042 
- DOI: https://doi.org/10.1016/s0969-2126(00)00066-6
- Primary Citation of Related Structures:  
1PGN, 1PGO, 1PGP, 1PGQ - PubMed Abstract: 
The nicotinamide adenine dinucleotide phosphate (NADP)-dependent oxidative decarboxylase, 6-phosphogluconate dehydrogenase, is a major source of reduced coenzyme for synthesis. Enzymes later in the pentose phosphate pathway convert the reaction product, ribulose 5-phosphate, to ribose 5-phosphate. Crystallographic study of complexes with coenzyme and substrate explain the NADP dependence which determines the enzyme's metabolic role and support the proposed general base-general acid mechanism.
Organizational Affiliation: 
University of Oxford, Laboratory of Molecular Biophysics, UK.