Characterization of unexplored amidohydrolase enzyme-pterin deaminase

Appl Microbiol Biotechnol. 2016 Jun;100(11):4779-89. doi: 10.1007/s00253-016-7513-9. Epub 2016 Apr 19.

Abstract

Pterin deaminase is an amidohydrolase enzyme hydrolyzing pteridines to form lumazine derivatives and ammonia. The enzyme captured the attention of scientists as early as 1959 and had been patented for its application as an anticancer agent. It is ubiquitously present in prokaryotes and has been reported in some eukaryotes such as honey bee, silkworm and rats. The enzyme has been observed to have a spectrum of substrates with the formation of respective lumazines. The role of the substrates of the enzyme in various metabolic pathways warrants a significant role in the biological activity of both prokaryotes and eukaryotes. Even though the functions of the enzyme have been explored in prokaryotes, their niche in the eukaryotic system is not clear. There is very few information on the structural and functional properties of the enzyme. This review has been congregated to emphasize the significance of pterin deaminase and analyzes the lacunae in understanding the biological characters of the enzyme.

Keywords: Amidohydrolase; Anticancer agent; Deamination; Lumazine; Pteridine; Pterin deaminase.

Publication types

  • Review

MeSH terms

  • Amidohydrolases / metabolism*
  • Aminohydrolases / antagonists & inhibitors
  • Aminohydrolases / metabolism*
  • Animals
  • Biopterins / analogs & derivatives
  • Biopterins / metabolism
  • Eukaryotic Cells / enzymology
  • Prokaryotic Cells / enzymology
  • Pteridines / chemistry

Substances

  • Pteridines
  • Biopterins
  • lumazine
  • Amidohydrolases
  • Aminohydrolases
  • pterin deaminase
  • sapropterin