Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis

Bioorg Chem. 2008 Feb;36(1):29-32. doi: 10.1016/j.bioorg.2007.10.005. Epub 2007 Dec 3.

Abstract

TenA catalyzes the hydrolysis of 4-amino-5-aminomethyl-2-methylpyrimidine and participates in the salvage of base-degraded thiamin. Here, we describe mutagenesis of the active site of TenA guided by structures of the enzyme complexed to a substrate analog and to the product. Catalytic roles for each of the active site residues are identified and a mechanism for the reaction is described.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Bacillus subtilis / enzymology*
  • Binding Sites
  • Catalysis
  • Hydrolases / chemistry
  • Hydrolases / genetics*
  • Hydrolases / isolation & purification
  • Hydrolysis
  • Models, Molecular
  • Molecular Structure
  • Mutagenesis, Site-Directed
  • Structure-Activity Relationship
  • Thiamine / chemistry
  • Thiamine / metabolism*

Substances

  • Hydrolases
  • thiaminase II
  • Thiamine