EC Number   |
General Information |
Reference |
|---|
    2.7.1.50 | evolution |
THI6 is a bifunctional enzyme found in the thiamin biosynthetic pathway in eukaryotes. In prokaryotes, thiamin phosphate synthase and 4-methyl-5-hydroxyethylthiazole kinase are separate gene products |
721627 |
| 2.7.1.50 | evolution |
three-quarters of the residues involved in interfacial regions are conserved, also the amino-acid residues in the nucleotide-binding, magnesium ion-binding and substrate-binding sites are conserved. The overall structure of PhThiK is similar to those of Bacillus subtilis ThiK (BsThiK) and Enterococcus faecalis V583 ThiK (EfThiK) |
-, 721209 |
| 2.7.1.50 | malfunction |
thiamin analogous compounds, when introduced into the vitamin B1 biosynthetic pathway and further converted into non-functional cofactors by the bacterium, can function as prodrugs which thus block various cofactor dependent pathways |
-, 760137 |
| 2.7.1.50 | metabolism |
enzyme ThiM is involved in the vitamin B1 (thiamin) biosynthetic pathway |
-, 760137 |
| 2.7.1.50 | metabolism |
THI6 is a bifunctional enzyme of the thiamin biosynthetic pathway |
721627 |
| 2.7.1.50 | more |
the enzyme topology shows the typical ribokinase fold of an alpha/beta protein. Binding of the nucleotide and substrate to the ThiK enzyme do not influence the trimeric quaternary association |
-, 721209 |
| 2.7.1.50 | physiological function |
enzyme ThiM is involved in the vitamin B1 (thiamin) biosynthetic pathway. Thiamin in its activated form, thiamin diphosphate, is an essential cofactor for all organisms |
-, 760137 |
| 2.7.1.50 | physiological function |
the N-terminal domain of THI6 catalyzes the ligation of the thiamin thiazole and pyrimidine moieties to form thiamin phosphate, and the C-terminal domain catalyzes the phosphorylation of 4-methyl-5-hydroxyethylthiazole in a salvage pathway |
721627 |
