Physarum polycephalum expresses a dihydropteridine reductase with selectivity for pterin substrates with a 6-(1', 2'-dihydroxypropyl) substitution

Biol Chem. 2003 Jul;384(7):1057-62. doi: 10.1515/BC.2003.118.

Abstract

Physarum polycephalum is one of few non-animal organisms capable of synthesizing tetrahydrobiopterin from GTP. Here we demonstrate developmentally regulated expression of quinoid dihydropteridine reductase (EC 1.6.99.7), an enzyme required for recycling 6,7-[8H]-dihydrobiopterin. Physarum also expresses phenylalanine-4-hydroxylase activity, an enzyme that depends on dihydropteridine reductase. The 24.4 kDa Physarum dihydropteridine reductase shares 43% amino acid identity with the human protein. A number of residues important for function of the mammalian enzyme are also conserved in the Physarum sequence. In comparison to sheep liver dihydropteridine reductase, purified recombinant Physarum dihydropteridine reductase prefers pterin substrates with a 6-(1', 2'-dihydroxypropyl) group. Our results demonstrate that Physarum synthesizes, utilizes and metabolizes tetrahydrobiopterin in a way hitherto thought to be restricted to the animal kingdom.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biopterins / analogs & derivatives*
  • Biopterins / chemistry
  • Biopterins / metabolism
  • Dihydropteridine Reductase / biosynthesis
  • Dihydropteridine Reductase / genetics
  • Dihydropteridine Reductase / metabolism*
  • Kinetics
  • Molecular Sequence Data
  • Phenylalanine Hydroxylase / biosynthesis
  • Phenylalanine Hydroxylase / metabolism
  • Phylogeny
  • Physarum polycephalum / enzymology*
  • Physarum polycephalum / genetics
  • Physarum polycephalum / growth & development
  • Pterins / chemistry
  • Pterins / metabolism*
  • Recombination, Genetic
  • Sequence Alignment
  • Substrate Specificity

Substances

  • Pterins
  • Biopterins
  • Phenylalanine Hydroxylase
  • Dihydropteridine Reductase
  • sapropterin