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Literature summary extracted from

  • Nishino, K.; Itokawa, Y.; Nishino, N.; Piros, K.; Cooper, J.R.
    Enzyme system involved in the synthesis of thiamin triphosphate. I. Purification and characterization of protein-bound thiamin diphosphate: ATP phosphoryltransferase (1983), J. Biol. Chem., 258, 11871-11878.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.4.15 additional information a low molecular weight cofactor is required Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.4.15 NEM 10 mM, 64% inhibition Bos taurus
2.7.4.15 PCMB 0.5 mM, 79.5% inhibition Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.4.15 0.6
-
 ATP pH 7.4, 37°C Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.15 Co2+ about 50% of the activation with Mg2+ Bos taurus
2.7.4.15 Mg2+ required Bos taurus
2.7.4.15 Mn2+ about 50% of the activation with Mg2+ Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.15 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.15
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.4.15 brain cortex Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.15 ATP + thiamine diphosphate
-
 Bos taurus ADP + thiamine triphosphate
-
 ?
2.7.4.15 CTP + thiamine diphosphate 6% of the activity with ATP Bos taurus CDP + thiamine triphosphate
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.15 7.5
-
 in Tris-HCl buffer slightly higher activity than in phosphate buffer Bos taurus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.4.15 Bos taurus isoelectric focusing
-
 5.1