3.6.1.28: thiamine-triphosphatase

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For detailed information about thiamine-triphosphatase, go to the full flat file.

Word Map on EC 3.6.1.28

3.6.1.28

adenylyl

electricus

electrophorus

phosphohydrolases

hydrophila

tdp

nitrosomonas

diphosphatase

triphosphorylated

Reaction

Synonyms

25 kDa thiamine triphosphatase, 25-kDa thiamine triphosphatase, phosphatase, thiamine tri-, thiamine triphosphatase, Thtpa, ThTPase, TTPase

ECTree

3 Hydrolases

3.6 Acting on acid anhydrides

3.6.1 In phosphorus-containing anhydrides

3.6.1.28 thiamine-triphosphatase

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Results	in table
7	Activating Compound
487	AA Sequence
1	CAS Registry Number
8	Cloned(Commentary)
2	Crystallization (Commentary)
3	Disease/ Diagnostics
2	General Stability
2	IC50 Value
62	Inhibitors
10	kcat/KM [mM/s]
5	Ki Value [mM]
47	KM Value [mM]
30	Localization
44	Metals/Ions
30	Molecular Weight [Da]
8	Natural Substrates/ Products (Substrates)
42	Organism
3	Pathway
9	PDB ID
22	pH Optimum
4	pH Range
15	Protein Variants
8	Purification (Commentary)
2	Reaction
1	Reaction Type
42	Reference
87	Source Tissue
44	Specific Activity [micromol/min/mg]
3	Storage Stability
75	Substrates and Products (Substrate)
6	Subunits
25	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
6	Temperature Stability [°C]
14	Turnover Number [1/s]

Subunits

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Subunits on EC 3.6.1.28 - thiamine-triphosphatase

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Mus musculus

Q8JZL3

x * 25000, enzyme solution structure determination by NMR spectroscopy, binding of Mg2+ induces only a minor local conformational change, whereas ThTP binding causes a more global conformational change, structural model for the mThTPase-ThTP-Mg2+ ternary complex, free mThTPase has an open cleft fold, the enzyme in the ternary complex adopts a tunnel fold, PDB ID 2JMU, overview

687693

monomer

5 entries