2.5.1.2: thiamine pyridinylase

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

Reaction

Synonyms

pyrimidine transferase, thiamin hydrolase, thiamin pyridinolase, thiamin pyridinylase, thiaminase, thiaminase I, thiamine pyridinolase, thiamine pyridinylase

ECTree

     2 Transferases

         2.5 Transferring alkyl or aryl groups, other than methyl groups

             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

                2.5.1.2 thiamine pyridinylase

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Results	in table
50	Activating Compound
111	AA Sequence
13	Application
1	CAS Registry Number
2	Cloned(Commentary)
2	Crystallization (Commentary)
21	General Information
62	Inhibitors
8	kcat/KM [mM/s]
2	Ki Value [mM]
62	KM Value [mM]
12	Localization
2	Metals/Ions
9	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
121	Organism
1	Oxidation Stability
2	Pathway
24	PDB ID
19	pH Optimum
5	pH Range
9	pH Stability
1	pI Value
7	Protein Variants
9	Purification (Commentary)
1	Reaction
1	Reaction Type
117	Reference
130	Source Tissue
4	Specific Activity [micromol/min/mg]
105	Substrates and Products (Substrate)
3	Subunits
28	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
17	Temperature Range [°C]
10	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.5.1.2 - thiamine pyridinylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

inactive C143S mutant with bound thiamine at 2.2 A resolution. Each monomer contains one thiamine molecule in a V-shaped cleft between the two domains. Tyrosine residues, Tyr46, Tyr48, Tyr80, Tyr252, Tyr269, and Tyr300, form an outer collar of the cleft with most of the active site residues located at the bottom of the cleft. The catalytic cysteine residue Cys143 is located on beta6

Clostridium botulinum

-

737686

by vapour-diffusion method

Paenibacillus thiaminolyticus

P45741

636858