Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.3 extracted from

  • Paul, D.; Chatterjee, A.; Begley, T.P.; Ealick, S.E.
    Domain organization in Candida glabrata THI6, a bifunctional enzyme required for thiamin biosynthesis in eukaryotes (2010), Biochemistry, 49, 9922-9934.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells [Candida] glabrata

Crystallization (Commentary)

Crystallization (Comment) Organism
unliganded and in complex with substrates and products, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.5), 0.2-0.25 M MgCl2, and 25-32% PEG400, at 4°C [Candida] glabrata

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ contains Mg2+ [Candida] glabrata

Organism

Organism UniProt Comment Textmining
[Candida] glabrata
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography [Candida] glabrata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)-thiazole
-
[Candida] glabrata thiamine phosphate + diphosphate
-
?
additional information the N-terminal domain of the bifunctional enzyme THI6 catalyzes the ligation of the thiamin thiazole and pyrimidine moieties to form thiamine phosphate, and the C-terminal domain catalyzes the phosphorylation of 4-methyl-5-hydroxyethylthiazole in a salvage pathway. Adenosine diphospho-5beta-ethyl-4-methylthiazole-2-carboxylic acid is not a substrate [Candida] glabrata ?
-
?

Subunits

Subunits Comment Organism
homohexamer
-
[Candida] glabrata

Synonyms

Synonyms Comment Organism
THI6 bifunctional enzyme [Candida] glabrata
thiamin phosphate synthase
-
[Candida] glabrata
TPS
-
[Candida] glabrata