EC Number   |
General Information |
Reference |
|---|
   2.5.1.2 | evolution |
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time |
759218 |
| 2.5.1.2 | malfunction |
thiaminase I is specifically implicated in thiamine deficiency syndromes in animals |
-, 758667 |
| 2.5.1.2 | metabolism |
the enzyme cleaves phosphorylated thiamine and toxic analogs, which releases precursors that can then be used for thiamine synthesis |
-, 758667 |
| 2.5.1.2 | physiological function |
although thiaminase I exposure does not stimulate the energy-sensing signaling kinases AKT, AMPK and GSK-3beta in MCF-7, ZR75, HS-578T and T-47D cell lines, thiaminase I exposure does stimulate expression of the ER stress response protein GRP78. Thiaminase I is cytotoxic in breast cancer cell lines and triggers the unfolded protein response |
711655 |
| 2.5.1.2 | physiological function |
Burkholderia pseudomallei possesses thiaminase I which catalyzes degradation of thiamine to 4-methyl-5-thiazoleethanol. ThiM, which encodes hydroxyethylthiazole kinase responsible for degradation of 4-methyl-5-thiazoleethanol, is absent or not expressed in all Burkholderia pseudomallei strains. The high 4-methyl-5-thiazoleethanol level in Burkholderia pseudomallei is likely due to the absence of hydroxyethylthiazole kinase and hence reduced downstream degradation |
737986 |
| 2.5.1.2 | physiological function |
Burkholderia thailandensis possesses thiaminase I which catalyzes degradation of thiamine to 4-methyl-5-thiazoleethanol. ThiM, which encodes hydroxyethylthiazole kinase responsible for degradation of 4-methyl-5-thiazoleethanol, is present and expressed in Burkholderia thailandensis |
737986 |
| 2.5.1.2 | physiological function |
crucian carp known to harbor thiaminase I activity are injected intramuscularly with live Aeromonas salmonicida. Significantly higher thiaminase activities are measured in all tissues of fish injected with live bacteria than in the control group. Different allocation pattern are shown: The amount of thiaminase I enzyme is elevated in the whole blood of injected fish in the absence of natural cosubstrate(s). The thiaminase activity of the injected, inflamed muscle suggests that both the amount of thiaminase enzyme and an unidentified natural cosubstrate(s) is elevated. This suggests that in addition to the enzyme, some cosubstrate(s) of fish or pathogen origin play a regulatory role in the physiological significance of thiaminase I activity in vivo |
704238 |
| 2.5.1.2 | physiological function |
thiaminase I provides a growth advantage by salvaging precursors from environmental thiamine and its analogs in Burkholderia thailandensis |
-, 758667 |
