Skip to main content

Structure of trifunctional THI20 from yeast

Buy Article:

$43.00 plus tax (Refund Policy)

In a recently characterized thiamin‐salvage pathway, thiamin‐degradation products are hydrolyzed by thiaminase II, yielding 4‐amino‐5‐hydroxymethyl‐2‐methylpyrimidine (HMP). This compound is an intermediate in thiamin biosynthesis that, once phosphorylated by an HMP kinase, can be used to synthesize thiamin monophosphate. Here, the crystal structure of Saccharomyces cerevisiae THI20, a trifunctional enzyme containing an N‐terminal HMP kinase/HMP‐P kinase (ThiD‐like) domain and a C‐terminal thiaminase II (TenA‐like) domain, is presented. Comparison to structures of the monofunctional enzymes reveals that while the ThiD‐like dimer observed in THI20 resembles other ThiD structures, the┬áTenA‐like domain, which is tetrameric in all previously reported structures, forms a dimer. Similarly, the active site of the ThiD‐like domain of THI20 is highly similar to other known ThiD enzymes, while the TenA‐like active site shows unique features compared with previously structurally characterized TenAs. In addition, a survey of known TenA structures revealed two structural classes, both of which have distinct conserved features. The TenA domain of THI20 possesses some features of both classes, consistent with its ability to hydrolyze both thiamin and the thiamin‐degradation product 2‐methyl‐4‐amino‐5‐aminomethylpyrimidine.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Document Type: Research Article

Publication date: 01 September 2011

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more