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2-northiamine + H2O
? + hydroxyethylthiazole
-
-
-
-
?
2-thiothiamine + H2O
?
-
-
-
-
?
4-amino-5-aminomethyl-2-methyl-pyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
4-amino-5-aminomethyl-2-methylpyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
the wild type enzyme is poorly active on 4-amino-5-aminoethyl-2-methylpyrimidine
-
-
?
4-amino-5-aminomethyl-2-methylpyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
dimethialium + H2O
?
-
-
-
-
?
oxythiamine + H2O
?
-
-
-
-
?
pyrimidinemethanol + aniline
pyrimidinemethylaniline + H2O
-
-
-
-
r
pyrithiamine + H2O
?
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
additional information
?
-
4-amino-5-aminomethyl-2-methyl-pyrimidine + H2O

4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
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
-
-
?
4-amino-5-aminomethyl-2-methyl-pyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
hydrolyzed more than two times faster than thiamine
-
-
?
4-amino-5-aminomethyl-2-methylpyrimidine + H2O

4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
-
-
-
-
?
4-amino-5-aminomethyl-2-methylpyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
-
-
-
?
4-amino-5-aminomethyl-2-methylpyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
-
-
-
-
?
oxothiamin + H2O

?
-
-
-
-
?
oxothiamin + H2O
?
-
-
-
?
oxythiamin + H2O

?
-
-
-
-
?
oxythiamin + H2O
?
-
-
-
?
thiamine + H2O

4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
r
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
ir
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
moulds
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
Trichosporon aneurinolyticum
-
-
-
-
?
additional information

?
-
the enzyme also catalyses the reaction of EC 2.7.4.7
-
-
-
additional information
?
-
-
no activity with N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine, thiamin monophosphate, thiamin diphosphate, thiamin disulfide, desthiothiamin, and thiochrome
-
-
-
additional information
?
-
no activity with N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine, thiamin monophosphate, thiamin diphosphate, thiamin disulfide, desthiothiamin, and thiochrome
-
-
-
additional information
?
-
Thi20p is involved in thiamine synthesis from pyrithiamine and oxythiamin
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
TenA does not accept TMP and TPP as substrates
-
-
-
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4-amino-5-aminomethyl-2-methyl-pyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
Q08224
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
-
-
?
4-amino-5-aminomethyl-2-methylpyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
additional information
?
-
4-amino-5-aminomethyl-2-methylpyrimidine + H2O

4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
-
-
-
-
?
4-amino-5-aminomethyl-2-methylpyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
P25052
-
-
-
?
4-amino-5-aminomethyl-2-methylpyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
-
-
-
-
?
oxothiamin + H2O

?
-
-
-
-
?
oxothiamin + H2O
?
P25052
-
-
-
?
oxythiamin + H2O

?
-
-
-
-
?
oxythiamin + H2O
?
P25052
-
-
-
?
thiamine + H2O

4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
r
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
P25052
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
moulds
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
Q08224
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
-
-
-
-
?
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
Trichosporon aneurinolyticum
-
-
-
-
?
additional information

?
-
-
no activity with N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine, thiamin monophosphate, thiamin diphosphate, thiamin disulfide, desthiothiamin, and thiochrome
-
-
-
additional information
?
-
P25052
no activity with N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine, thiamin monophosphate, thiamin diphosphate, thiamin disulfide, desthiothiamin, and thiochrome
-
-
-
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
-
-
-
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0.0046
-
in 100 mM Tris-HCl, pH 7.5, at 37°C
0.091
-
with oxothiamin as substrate, at 30°C in 45 mM Tris/HCl buffer, pH 7.5, containing 0.9 mM dithiothreitol and 0.45 M glycinebetaine
0.162
-
with thiamine as substrate, at 30°C in 45 mM Tris/HCl buffer, pH 7.5, containing 0.9 mM dithiothreitol and 0.45 M glycinebetaine
0.205
-
with oxythiamin as substrate, at 30°C in 45 mM Tris/HCl buffer, pH 7.5, containing 0.9 mM dithiothreitol and 0.45 M glycinebetaine
0.292
-
with 4-amino-5-aminomethyl-2-methylpyrimidine as substrate, at 30°C in 45 mM Tris/HCl buffer, pH 7.5, containing 0.9 mM dithiothreitol and 0.45 M glycinebetaine
additional information
-
mean thiaminase activity in the alewives studied increases from 6.9 to 16.0 nmol/min/g from the time of their collection in Cayuga lake to the start of laboratory experiments 1.5-2.5 years later, the latter value is more than twice that of previously reported levels of thiaminase activity from alewives collected in the wild, data suggest that the variability in thiaminase activity is not related to stress from salt reduction or food limitation; whole body activity is measured, no significant diferrences in thiaminase activity are found between the control fishes and the alewives which are exposed to food limitation and reduced salt content in the water
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dialyzing the purified enzyme solution against 52% saturated ammonium sulfate solution, two weeks
-
hanging drop vapour diffusion method
-
vapor diffusion method, using 0.1 m Tris (pH 8.5), 1.1 M lithium sulfate
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
-
hanging drop vapor diffusion method
-
purified recombinant C-terminally Strep-tagged TenA, hanging drop vapour diffusion method, 0.002 ml of 10 mg/ml protein in 100 mM Tris-HCl buffer pH 8.0, is mixed with 0.002 l of reservoir solution containing 0.2 M sodium acetate, 0.1 M Tris-HCl pH 8.5 and 28% w/v PEG 3350, 20°C, 7 days, X-ray diffraction structure determination and analysis at 2.60 A resolution, molecular replacement, modelling
-
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Kimura, Y.; Iwashima, A.
Occurence of thiaminase II in Saccharomyces cerevisiae
Experientia
43
888-890
1987
Saccharomyces cerevisiae
brenda
Abe, M.; Nishimune, T.; Ito, S.; Kimoto, M.; Hayashi, R.
A simple method for the detection of two types of thiaminase-producing colonies
FEMS Microbiol. Lett.
34
129-133
1986
Aneurinibacillus aneurinilyticus
-
brenda
Murata, K.
Action of two types of thiaminase on thiamine and its analogues
Ann. N. Y. Acad. Sci.
378
146-156
1982
Aneurinibacillus aneurinilyticus
brenda
Edwin, E.E.
Determination of thiaminase activity using thiazole-labeled thiamine
Methods Enzymol.
62
113-117
1979
Aneurinibacillus aneurinilyticus
brenda
Fujita, A.
Recollections of the background of the study on thiaminase and thermostable thiamine-decomposing factor in Japan
J. Vitaminol. (Kyoto)
18
67-72
1972
Aneurinibacillus aneurinilyticus, moulds
brenda
Wittliff, J.L.; Airth, R.L.
Thiaminase II (thiamine hydrolase, EC 3.5.99.2)
Methods Enzymol.
18
234-238
1971
Aneurinibacillus aneurinilyticus, Candida sp. (in: Saccharomycetales), Geotrichum candidum, Trichosporon aneurinolyticum
-
brenda
Ikehata, H.
The purification of thiaminase II
J. Gen. Appl. Microbiol.
6
30-39
1960
Aneurinibacillus aneurinilyticus
-
brenda
Fujita, A.; Nose, Y.; Kuratani, K.
The second type of bacterial thiaminase
J. Vitaminol. (Kyoto)
1
1-7
1954
Aneurinibacillus aneurinilyticus
brenda
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
brenda
Toms, A.V.; Haas, A.L.; Park, J.H.; Begley, T.P.; Ealick, S.E.
Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II
Biochemistry
44
2319-2329
2005
Bacillus subtilis, Bacillus subtilis (P25052)
brenda
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
brenda
Lepak, J.M.; Kraft, C.E.; Honeyfield, D.C.; Brown, S.B.
Evaluating the effect of stressors on thiaminase activity in alewife
J. Aquat. Anim. Health
20
63-71
2008
Alosa pseudoharengus
brenda
Barison, N.; Cendron, L.; Trento, A.; Angelini, A.; Zanotti, G.
Structural and mutational analysis of TenA protein (HP1287) from the Helicobacter pylori thiamin salvage pathway - evidence of a different substrate specificity
FEBS J.
276
6227-6235
2009
Helicobacter pylori, Helicobacter pylori (O25874)
brenda
Mueller, I.B.; Bergmann, B.; Groves, M.R.; Couto, I.; Amaral, L.; Begley, T.P.; Walter, R.D.; Wrenger, C.
The vitamin B1 metabolism of Staphylococcus aureus is controlled at enzymatic and transcriptional levels
PLoS ONE
4
e7656
2009
Staphylococcus aureus
brenda
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
brenda
Begum, A.; Drebes, J.; Perbandt, M.; Wrenger, C.; Betzel, C.
Purification, crystallization and preliminary X-ray diffraction analysis of the thiaminase type II from Staphylococcus aureus
Acta Crystallogr. Sect. F
67
51-53
2011
Staphylococcus aureus
brenda
Begum, A.; Drebes, J.; Kikhney, A.; Mueller, I.B.; Perbandt, M.; Svergun, D.; Wrenger, C.; Betzel, C.
Staphylococcus aureus thiaminase II: oligomerization warrants proteolytic protection against serine proteases
Acta Crystallogr. Sect. D
69
2320-2329
2013
Staphylococcus aureus
brenda
Zallot, R.; Yazdani, M.; Goyer, A.; Ziemak, M.J.; Guan, J.C.; McCarty, D.R.; de Crecy-Lagard, V.; Gerdes, S.; Garrett, T.J.; Benach, J.; Hunt, J.F.; Shintani, D.K.; Hanson, A.D.
Salvage of the thiamin pyrimidine moiety by plant TenA proteins lacking an active-site cysteine
Biochem. J.
463
145-155
2014
Bacillus subtilis 168 (P25052), Bacillus subtilis (P25052)
brenda