2.7.1.49: hydroxymethylpyrimidine kinase
This is an abbreviated version!
For detailed information about hydroxymethylpyrimidine kinase, go to the full flat file.
Word Map on EC 2.7.1.49
Reaction
Synonyms
4-amino-5-hydroxymethyl-2-methyl pyrimidine kinase, 4-amino-5-hydroxymethyl-2-methylpyrimidine (phosphate) kinase, 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase, 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate kinase, EC 2.7.1.14, EC 2.7.1.35, HMP kinase, HMP-P kinase, HMP/HMP phosphate kinase, HMP/HMP-P kinase, HMPK, HMPPK, HVO_2666, hydroxymethylpyrimidine kinase (phosphorylating), hydroxymethylpyrimidine phosphate kinase, More, pyridoxal kinase, SAV0580, StHMPPK, Thi20, Thi20p, THI3, ThiD, TTHA0680, TtHMPPK
ECTree
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Engineering on EC 2.7.1.49 - hydroxymethylpyrimidine kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C110A
residue C110 is mandatory for pyridoxal, but not for pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine turnover
C214A
mutant does not turn over pyridoxal, pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine. Residue C214 acts as the catalytic base in the phosphorylation reaction
C110A
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residue C110 is mandatory for pyridoxal, but not for pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine turnover
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C214A
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mutant does not turn over pyridoxal, pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine. Residue C214 acts as the catalytic base in the phosphorylation reaction
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additional information
additional information
construction of a thiD knockout mutant strain, complementation of the Escherichia coli DELTA thiD knockout mutant is possible by heterologous expression of gene ThiD2, ThiD2 proteins catalyze phosphorylation of HMP monophosphate, but not of HMP or its toxic analogues and damage products such as bacimethrin and 5-(hydroxymethyl)-2-methylpyrimidin-4-ol. As strictly monofunctional HMP monophosphate kinases (EC 2.7.4.7), ThiD2 proteins eliminate a potentially fatal vulnerability of canonical ThiD, at the cost of the ability to reclaim HMP formed by thiamin turnover
additional information
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construction of a thiD knockout mutant strain, complementation of the Escherichia coli DELTA thiD knockout mutant is possible by heterologous expression of gene ThiD2, ThiD2 proteins catalyze phosphorylation of HMP monophosphate, but not of HMP or its toxic analogues and damage products such as bacimethrin and 5-(hydroxymethyl)-2-methylpyrimidin-4-ol. As strictly monofunctional HMP monophosphate kinases (EC 2.7.4.7), ThiD2 proteins eliminate a potentially fatal vulnerability of canonical ThiD, at the cost of the ability to reclaim HMP formed by thiamin turnover
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additional information
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phosphomethylpyrimidine kinase activity, EC 2.7.4.7, is abolished in C-terminally truncated isozymes Thi20p and Thi21p, the mutant yeast strains sow no thiamin phosphate synthesis activity
additional information
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phosphomethylpyrimidine kinase activity, EC 2.7.4.7, is abolished in C-terminally truncated isozymes Thi20p and Thi21p, the mutant yeast strains sow no thiamin phosphate synthesis activity
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