Gene ytkD of Bacillus subtilis encodes an atypical nucleoside triphosphatase member of the Nudix hydrolase superfamily

J Bacteriol. 2004 Dec;186(24):8380-4. doi: 10.1128/JB.186.24.8380-8384.2004.

Abstract

Gene ytkD of Bacillus subtilis, a member of the Nudix hydrolase superfamily, has been cloned and expressed in Escherichia coli. The purified protein has been characterized as a nucleoside triphosphatase active on all of the canonical ribo- and deoxyribonucleoside triphosphates. Whereas all other nucleoside triphosphatase members of the superfamily release inorganic pyrophosphate and the cognate nucleoside monophosphate, YtkD hydrolyses nucleoside triphosphates in a stepwise fashion through the diphosphate to the monophosphate, releasing two molecules of inorganic orthophosphate. Contrary to a previous report, our enzymological and genetic studies indicate that ytkD is not an orthologue of E. coli mutT.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / enzymology
  • Bacillus subtilis / genetics*
  • Bacterial Proteins* / chemistry
  • Bacterial Proteins* / genetics
  • Bacterial Proteins* / isolation & purification
  • Bacterial Proteins* / metabolism
  • Cloning, Molecular
  • Escherichia coli Proteins / genetics
  • Genetic Complementation Test
  • Molecular Sequence Data
  • Nucleoside-Triphosphatase* / chemistry
  • Nucleoside-Triphosphatase* / genetics
  • Nucleoside-Triphosphatase* / isolation & purification
  • Nucleoside-Triphosphatase* / metabolism
  • Nudix Hydrolases
  • Phosphoric Monoester Hydrolases / genetics
  • Pyrophosphatases / chemistry*
  • Pyrophosphatases / genetics
  • Sequence Analysis, DNA
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Phosphoric Monoester Hydrolases
  • Pyrophosphatases
  • mutT protein, E coli
  • Nucleoside-Triphosphatase