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Literature summary for 3.5.99.2 extracted from

  • French, J.B.; Begley, T.P.; Ealick, S.E.
    Structure of trifunctional THI20 from yeast (2011), Acta Crystallogr. Sect. D, 67, 784-791.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of C-terminally His6-tagged THI20 in Escherichia coli strain BL21 (DE3) Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant C-terminally His6-tagged THI20, hanging drop vapour diffusion method, 10 mg/ml protein in 10 mM Tris buffer, pH 7.6, with 30 mM NaCl, is mixed with 10-14% PEG 8000, 0.2 M calcium acetate, and 0.1 M imidazole, pH 7.5, microseeding, 2-3 days, X-ray diffraction structure determination and analysis at 2.68 A resolution, molecular replacement, modelling Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae THI20 is a trifunctional enzyme that is composed of a ThiD-like N-terminal domain that catalyzes the phosphorylation of 4-amino-5-hydroxymethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate and of 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate to 4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphate, and a TenA-like C-terminal domain with thiaminase activity ?
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His6-tagged THI20 from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information THI20 is a trifunctional enzyme that is composed of a ThiD-like N-terminal domain that catalyzes the phosphorylation of 4-amino-5-hydroxymethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate and of 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate to 4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphate, and a TenA-like C-terminal domain with thiaminase activity Saccharomyces cerevisiae ?
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additional information thiamin-degradation products are hydrolyzed by thiaminase II yielding 4-amino-5-hydroxymethyl-2-methylpyrimidine. HMP. The C-terminal domain is homologous to Bacillus subtilis TenA, which catalyzes the production of HMP from thiamin degradation products in the salvage pathway Saccharomyces cerevisiae ?
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Subunits

Subunits Comment Organism
dimer overall dimeric organization in which N-terminal domains and C-terminal domains form ThiD-like and TenA-like local dimers, A relatively flexible linker region composed of a loop and a short helix joins the two domains, domain organization, overview Saccharomyces cerevisiae
More THI20 is a trifunctional enzyme containing an N-terminal HMP kinase/HMP-P kinase (ThiD-like) domain and a C-terminal thiaminase II (TenA-like) domain. The ThiD-like dimer observed in THI20 resembles other ThiD structures, the TenA-like domain, which is tetrameric in all previously reported structures, forms a dimer Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Thi20
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Saccharomyces cerevisiae
thiaminase II
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Saccharomyces cerevisiae

General Information

General Information Comment Organism
metabolism thiamin-degradation products are hydrolyzed by thiaminase II, yielding 4-amino-5-hydroxymethyl-2-methylpyrimidine. This compound is an intermediate in thiamin biosynthesis. The enzyme is involved in the biosynthesis of thiamin diphosphate, the active form of the cofactor Saccharomyces cerevisiae
additional information THI20 is a trifunctional enzyme containing an N-terminal HMP kinase/HMP-P kinase (ThiD-like) domain and a C-terminal thiaminase II (TenA-like) domain Saccharomyces cerevisiae