2.7.6.2: thiamine diphosphokinase
This is an abbreviated version!
For detailed information about thiamine diphosphokinase, go to the full flat file.
Word Map on EC 2.7.6.2
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2.7.6.2
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pyrophosphate
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dihydropteroate
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pyrophosphorylated
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tdp
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ribosephosphate
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hydroxymethyldihydropterin
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pyrithiamine
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6-hydroxymethyl-7,8-dihydropterin
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dihydroneopterin
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thiamine-responsive
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oxythiamine
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megaloblastic
-
medicine
- 2.7.6.2
- pyrophosphate
- dihydropteroate
-
pyrophosphorylated
- tdp
-
ribosephosphate
-
hydroxymethyldihydropterin
- pyrithiamine
- 6-hydroxymethyl-7,8-dihydropterin
- dihydroneopterin
-
thiamine-responsive
- oxythiamine
-
megaloblastic
- medicine
Reaction
Synonyms
At1g02880 (AtTPK1), At2g44750 (AtTPK2), ATP:thiamin pyrophosphotransferase, CA1462, hTPK1, Plasmodium falciparum thiamine pyrophosphokinase, pyrophosphokinase, pyrophosphokinase, thiamin, TDPK, thiamin kinase, thiamin pyrophosphokinase, thiamin pyrophosphotransferase, thiamin:ATP pyrophosphotransferase, thiamine diphosphokinase, thiamine kinase, thiamine pyrophokinase, thiamine pyrophosphokinase, thiaminokinase, TPK, Tpk1, TPTase, YcfN
ECTree
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Metals Ions
Metals Ions on EC 2.7.6.2 - thiamine diphosphokinase
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Co2+
Mg2+
Mn2+
Zn2+
Co2+
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absolute requirement for a divalent cation such as Mg2+, Mn2+ or Co2+. In presence of 2 mM ATP maximal activity occurs with 1 mM Co2+
Mg2+
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ligands electronic density map and Mg2+ coordination structure, the delta-oxygen from D113 and D115 and one oxygen atom from each phosphate group of the thiamine-PNP. The last coordination of this Mg2+ involves an oxygen atom from the free inorganic phosphate, overview
Mg2+
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absolute requirement for a divalent cation such as Mg2+, Mn2+ or Co2+. In presence of 2 mM ATP maximal activity occurs with above 3 mM Mg2+
Mg2+
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for optimal activity the ratio of magnesium to ATP must be fixed at 0.6. The Mg(ATP)26- species might by the actual diphosphoryl donor
Mn2+
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absolute requirement for a divalent cation such as Mg2+, Mn2+ or Co2+. In presence of 2 mM ATP maximal activity occurs with 0.5 mM Mn2+
Mn2+
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Substitution of magnesium by Mn2+ decreases the enzyme activity by 42%.
Zn2+
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Substitution of magnesium by Zn2+ decreases the enzyme activity by 85%.