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Information on EC 3.5.99.2 - aminopyrimidine aminohydrolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q08224

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IUBMB Comments
Previously known as thiaminase II, this enzyme is involved in the regeneration of the thiamine pyrimidine from degraded products, rather than in thiamine degradation, and participates in thiamine salvage pathways.
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Saccharomyces cerevisiae
UNIPROT: Q08224
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
thiaminase, thi20, thiaminase ii, thi20p, tena_c, thiaminase type ii, hp1287, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thiaminase II
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-N bond
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-amino-5-aminomethyl-2-methylpyrimidine aminohydrolase
Previously known as thiaminase II, this enzyme is involved in the regeneration of the thiamine pyrimidine from degraded products, rather than in thiamine degradation, and participates in thiamine salvage pathways.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-80-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-amino-5-aminomethyl-2-methyl-pyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
show the reaction diagram
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
show the reaction diagram
2-northiamine + H2O
? + hydroxyethylthiazole
show the reaction diagram
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?
dimethialium + H2O
?
show the reaction diagram
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?
oxythiamine + H2O
?
show the reaction diagram
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-
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?
pyrithiamine + H2O
?
show the reaction diagram
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?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-amino-5-aminomethyl-2-methyl-pyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
show the reaction diagram
physiological substrate, hydrolyzed more than two times faster than thiamine. Thiaminase II activity of Thi20p is involved in the thiamine salvage pathway by catalyzing the hydrolysis of 4-amino-5-hydroxymethyl-2-methylpyrimidine precursors in Saccharomyces cerevisiae
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?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
show the reaction diagram
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-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
show the reaction diagram
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?
additional information
?
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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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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
thi20 deletion mutant cells can not grow in the presence of the synthetic thiamine antagonists, pyrithiamine and oxythiamin, indicating that the THI20 gene is necessary for the utilization of pyrithiamine and oxythiamine as precursors for thiamin
physiological function
thiaminase II activity of Thi20p is involved in the thiamine salvage pathway
metabolism
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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
additional information
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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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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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
additional information
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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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged THI20 from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
expression of C-terminally His6-tagged THI20 in Escherichia coli strain BL21 (DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kimura, Y.; Iwashima, A.
Occurence of thiaminase II in Saccharomyces cerevisiae
Experientia
43
888-890
1987
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Haas, A.L.; Laun, N.P.; Begley, T.P.
Thi20, a remarkable enzyme from Saccharomyces cerevisiae with dual thiamin biosynthetic and degradation activities
Bioorg. Chem.
33
338-344
2005
Saccharomyces cerevisiae (Q08224), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Onozuka, M.; Konno, H.; Kawasaki, Y.; Akaji, K.; Nosaka, K.
Involvement of thiaminase II encoded by the THI20 gene in thiamin salvage of Saccharomyces cerevisiae
FEMS Yeast Res.
8
266-275
2008
Saccharomyces cerevisiae (Q08224), Saccharomyces cerevisiae
Manually annotated by BRENDA team
French, J.B.; Begley, T.P.; Ealick, S.E.
Structure of trifunctional THI20 from yeast
Acta Crystallogr. Sect. D
67
784-791
2011
Saccharomyces cerevisiae
Manually annotated by BRENDA team