EC Number   |
General Information |
Reference  |
|---|
    2.7.1.49 | more |
experimental resurrection of the last common ancestor of the hydroxymethyl pyrimidine kinase group based on comparison of hydroxymethyl pyrimidine and pyridoxal kinases. Probably the last common ancestor was not able to use pyridoxal under physiological conditions. The pyridoxal kinase activity present in the current bifunctional enzymes must have appeared in a convergent event independently of the pyridoxal kinase activity of pdxY and pdxK genes. Substrate pyridoxal is 8-times less preferred than the phosphorylation of hydroxymethyl pyrimidine by the last ancestor |
-, 738234 |
| 2.7.1.49 | metabolism |
the salvage of HMP is accomplished by its phosphorylation to HMP-P by the HMP kinase activity (HMPK) |
-, 758702 |
| 2.7.1.49 | more |
molecular dynamics simulation shows that Salmonella typhimurium StHMPPK and Thermus thermophilus TtHMPPK have striking differences in their conformational flexibility, which can be correlated with the hydrophobic packing and electrostatic interaction network given mainly by salt bridge bonds, but interestingly not by the number of hydrogen bond interactions as reported for other thermophilic enzymes, stucture comparisons, all-atom explicit solvent molecular dynamics simulation of StHMPPK and TtHMPPK, overview |
-, 758702 |
| 2.7.1.49 | physiological function |
the enzyme catalyzes an essential step for the biosynthesis of thiamin pyrophosphate |
-, 758702 |
| 2.7.1.49 | physiological function |
the hydroxymethylpyrimidine phosphate kinases (HMPPK) encoded by the thiD gene are involved in the thiamine biosynthesis pathway, can perform two consecutive phosphorylations of 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) and are found in thermophilic and mesophilic bacteria. The enzyme StHMPPK is able to catalyze two related reactions in consecutive steps, besides the phosphorylation of HMP to give HMP-P, the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK, EC 2.7.4.7) being this last reaction an essential step for the biosynthesis of thiamin diphosphate |
-, 758702 |
| 2.7.1.49 | physiological function |
the hydroxymethylpyrimidine phosphate kinases (HMPPK) encoded by the thiD gene are involved in the thiamine biosynthesis pathway, can perform two consecutive phosphorylations of 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) and are found in thermophilic and mesophilic bacteria. The enzyme TtHMPPK is able to catalyze two related reactions in consecutive steps, besides the phosphorylation of HMP to give HMP-P, the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK, EC 2.7.4.7) being this last reaction an essential step for the biosynthesis of thiamin diphosphate |
-, 758702 |
| 2.7.1.49 | evolution |
ThiD is a member of the ribokinase family, but differs from other members in catalyzing two consecutive phosphorylations. The other members of the family catalyze only the phosphorylation of a hydroxymethyl group to give a monophosphate, i.e. the equivalent of the HMP kinase reaction. The HMP kinase activity of ThiD is hence presumably ancestral and the HMP-P kinase activity is an evolutionary novelty |
-, 758754 |
| 2.7.1.49 | metabolism |
the enzyme takes part in the bacterial thiamin biosynthesis and salvage pathways, overview |
-, 758754 |
| 2.7.1.49 | physiological function |
the bifunctional canonical kinase (ThiD) that converts the thiamin biosynthesis intermediate hydroxymethylpyrimidine (HMP) monophosphate into the diphosphate (EC 2.7.4.7) can also very efficiently convert free HMP into the monophosphate (EC 2.7.1.49) in prokaryotes, plants, and fungi. This HMP kinase activity enables salvage of HMP, but it is not substrate-specific and so allows toxic HMP analogues and damage products to infiltrate the thiamin biosynthesis pathway |
-, 758754 |
| 2.7.1.49 | evolution |
ThiN is a versatile domain of transcriptional repressors and catalytic enzymes of thiamine biosynthesis in archaea, residues that distinguish catalytic from noncatalytic ThiN domains, overview. Structural architecture comparisons of ThiD, ThiE, and ThiN domain-containing proteins in select haloarchaea |
-, 759429 |
