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Literature summary for 2.7.4.15 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

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
brain cortex Bos taurus
-

Substrates and Products (Substrate)

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

pH Optimum

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

pI Value

Organism Comment pI Value Maximum pI Value
Bos taurus isoelectric focusing
-
5.1