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PGD  -  phosphogluconate dehydrogenase

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Disease relevance of 6-PGDH


High impact information on 6-PGDH

  • The structure has refined to R=18.6% (Rfree=27.3%) with good geometry.The amino acid sequence of T. brucei 6PGDH is only 35% identical to that of the sheep liver enzyme and significant activity differences have been observed [2].
  • Crystal structures of 6-phosphogluconate dehydrogenase (6PGDH) from sheep liver indicate that S128 and N187 are within hydrogen-bonding distance of 6PG in the E:6PG binary complex and NADPH in the E:NADPH binary complex [3].
  • Data are consistent with a significant role of M13 in the orientation of the cofactor nicotinamide ring in the mechanism of 6PGDH, likely with respect to geometry and distance of the ring from C3 of 6PG [4].
  • A methionine side chain (Met13) interacts with the si face of NADP(+) in the complex with the oxidized coenzyme, is likely to affect the binding mode of the nicotinamide ring of NADP(+), and may play a role in catalysis in the 6PGDH reaction [4].
  • A second 6-PGDH gene has been identified from the genome of B. subtilis [1].

Biological context of 6-PGDH

  • The model systems we choose for the enzyme contain the essential parts of the cofactor (NADP+), the substrate 6-phosphogluconate (6PG), and some key residues (Lys183 and Glu190) in the active site of sheep liver 6PGDH [5].

Associations of 6-PGDH with chemical compounds

  • Sheep liver 6-phosphogluconate dehydrogenase (6-PGDH) is an enzyme of the pentose phosphate pathway [6].
  • A two-step procedure for the purification of 6-phosphogluconate dehydrogenase (EC; 6-PGDH) from sheep liver is described [7].
  • The crystal structure of sheep liver 6-phosphogluconate dehydrogenase (6PGDH) shows marked differences in the position of the nicotinamide mononucleotide (NMN) moiety of NADP(+) and NADPH (Adams, J. M., Grant, H. E., Gover, S., Naylor, C. E., and Phillips, C. (1994) Structure 2, 651-668) [4].

Other interactions of 6-PGDH

  • Postmortem longissimus muscle, s.c. fat, intermuscular fat (INT), and kidney fat (KP) samples were assayed in vitro for glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH) activity (nanomoles.minute-1.gram of tissue-1), and samples were subjected to electrophoresis (PAGE) to separate tissue-specific isoforms [8].


  1. 6-Phosphogluconate dehydrogenase from Lactococcus lactis: a role for arginine residues in binding substrate and coenzyme. Tetaud, E., Hanau, S., Wells, J.M., Le Page, R.W., Adams, M.J., Arkison, S., Barrett, M.P. Biochem. J. (1999) [Pubmed]
  2. A 2.8 A resolution structure of 6-phosphogluconate dehydrogenase from the protozoan parasite Trypanosoma brucei: comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues. Phillips, C., Dohnalek, J., Gover, S., Barrett, M.P., Adams, M.J. J. Mol. Biol. (1998) [Pubmed]
  3. Role of the s128, h186, and n187 triad in substrate binding and decarboxylation in the sheep liver 6-phosphogluconate dehydrogenase reaction. Li, L., Zhang, L., Cook, P.F. Biochemistry (2006) [Pubmed]
  4. Role of methionine-13 in the catalytic mechanism of 6-phosphogluconate dehydrogenase from sheep liver. Cervellati, C., Dallocchio, F., Bergamini, C.M., Cook, P.F. Biochemistry (2005) [Pubmed]
  5. Catalytic mechanism of 6-phosphogluconate dehydrogenase: a theoretical investigation. Wang, J., Li, S. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical. (2006) [Pubmed]
  6. Sheep 6-phosphogluconate dehydrogenase. Revised protein sequence based upon the sequences of cDNA clones obtained with the polymerase chain reaction. Somers, D.O., Medd, S.M., Walker, J.E., Adams, M.J. Biochem. J. (1992) [Pubmed]
  7. A two-step purification procedure for sheep liver 6-phosphogluconate dehydrogenase. Somers, D.O., Hajdu, J., Adams, M.J. Protein Expr. Purif. (1991) [Pubmed]
  8. Tissue-specific activity of pentose cycle oxidative enzymes during feeder lamb development. Belk, K.E., Savell, J.W., Davis, S.K., Taylor, J.F., Womack, J.E., Smith, S.B. J. Anim. Sci. (1993) [Pubmed]
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