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Information on EC 3.5.99.2 - aminopyrimidine aminohydrolase
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3.5.99.2 aminopyrimidine aminohydrolaseIUBMB 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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Word Map
- 3.5.99.2
- transketolase
- thiaminolyticus
-
polioencephalomalacia
-
cerebrocortical
-
tenas
- pseudoharengus
-
alosa
- 4-amino-5-hydroxymethyl-2-methylpyrimidine
- venerupis
- decussata
- shad
-
dorosoma
-
2.5.1.2
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
HP1287, TenA, TenA_C, Thi20, Thi20p, thiaminase, thiaminase II, thiaminase type II, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
TenA
TenA_C
Thi20
thiaminase
thiaminase II
thiaminase II
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
(1)
-
-
-
thiamine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
(2)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-N bond
hydrolysis of C-N bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9024-80-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
pyrimidinemethanol + aniline
pyrimidinemethylaniline + H2O
-
-
-
-
r
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
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
-
-
-
-
?
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
-
-
-
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
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
-
-
-
-
?
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
?
-
-
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
?
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-methylpyrimidine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + NH3
thiamine + H2O
4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole
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
-
-
-
-
?
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
-
-
-
?
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
?
-
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
?
-
-
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
inhibited by many aromatic and heterocyclic amines
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
in a concentration range of 0.02 mM to 1000 mM
L-cysteine
-
in a concentration range of 0.02 mM to 1000 mM
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Ataxia
Thiamin is decomposed due to Anaphe spp. entomophagy in seasonal ataxia patients in Nigeria.
Avitaminosis
Prenatal exposure of a girl with autism spectrum disorder to 'horsetail' (Equisetum arvense) herbal remedy and alcohol: a case report.
Breast Neoplasms
Metabolic effects of acute thiamine depletion are reversed by rapamycin in breast and leukemia cells.
Communicable Diseases, Emerging
Resurgence of Salmonid Herpesvirus-3 Infection (Epizootic Epitheliotropic Disease) in Hatchery-Propagated Lake Trout in Michigan.
Leukemia
Metabolic effects of acute thiamine depletion are reversed by rapamycin in breast and leukemia cells.
Leukemia
Pharmacologic properties of polyethylene glycol-modified Bacillus thiaminolyticus thiaminase I enzyme.
Neoplasms
Population thiamine status and varying cancer rates between western, Asian and African countries.
Thiamine Deficiency
Cerebrocortical necrosis in ruminants: effect of thiaminase type 1-producing Clostridium sporogenes in lambs.
Thiamine Deficiency
Clinical evaluation and biochemical analyses of thiamine deficiency in Pacific harbor seals (Phoca vitulina) maintained at a zoological facility.
Thiamine Deficiency
Comparison of thiaminase activity in fish using the radiometric and 4-nitrothiophenol colorimetric methods.
Thiamine Deficiency
Expression of Thiaminase in Zebrafish (Danio rerio) is Lethal and Has Implications for Use as a Biocontainment Strategy in Aquaculture and Invasive Species.
Thiamine Deficiency
Faecal thiaminase, plasma lactate and pyruvate concentrations and erythrocyte transketolase activity changes in apparently normal replacement ewes after the initiation to the pasture.
Thiamine Deficiency
Gizzard shad thiaminase activity and its effect on the thiamine status of captive American alligators Alligator mississippiensis.
Thiamine Deficiency
Studies on the thiamine deficiency due to bacterial thiaminase. II. Experiments on hens.
Thiamine Deficiency
Studies on the thiamine deficiency due to bacterial thiaminase. I. Investigations on intestinal contents.
Thiamine Deficiency
Studies on thiamine deficiency due to bacterial thiaminase. III. Further investigations on thiaminase disease.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.058
4-amino-5-aminomethyl-2-methylpyrimidine
wild type enzyme, in 30 mM Tris, 50 mM NaCl (pH 8.0), at 20°C
0.068
4-amino-5-aminomethyl-2-methylpyrimidine
mutant enzyme F47Y, in 30 mM Tris, 50 mM NaCl (pH 8.0), at 20°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
4-amino-5-aminomethyl-2-methylpyrimidine
mutant enzyme F47Y, in 30 mM Tris, 50 mM NaCl (pH 8.0), at 20°C
0.003
4-amino-5-aminomethyl-2-methylpyrimidine
wild type enzyme, in 30 mM Tris, 50 mM NaCl (pH 8.0), at 20°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
additional information
-
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
trifunctional enzyme EC 3.5.99.2/EC 2.7.1.49/EC 2.7.4.7
SwissProt
brenda
trifunctional enzyme: EC 3.5.99.2/EC 2.7.1.49/EC 2.7.4.7
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
metabolism
physiological function
thiaminase II activity of Thi20p is involved in the thiamine salvage pathway
additional information
metabolism
TenA plays a pivotal role in the thiamin biosynthetic route
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
metabolism
-
thiaminase type II, TenA, catalyzes the deamination of aminopyrimidines, including the cleavage of thiamine to 4-amino-5-hydroxymethyl-2-methylpyrimidine and 5-(2-hydroxyethyl)-4-methylthiazole in the metabolism of thiamine (vitamin B1), in Staphylococcus aureus
additional information
-
putative active-site residues are Asp44, Cys137, Tyr167 and Glu208
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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
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. 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
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
dialyzing the purified enzyme solution against 52% saturated ammonium sulfate solution, two weeks
-
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
-
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F47Y
poorly active mutant. At pH 6.0, its activity is absent. Moreover, the enzyme does not present any activity on thiamin degradation
D111A/K115A
-
the activity of the monomeric mutant is not significantly altered in comparison to the wild type enzyme
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
80
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-Sepharose column chromatography and Superdex 200 gel filtration
recombinant C-terminally His6-tagged THI20 from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration
-
recombinant C-terminally Strep-tagged TenA from Escherichia coli strain BL21(DE3) by affinity chromatography
-
Strep-Tactin Sepharose column chromatography and Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of C-terminally His6-tagged THI20 in Escherichia coli strain BL21 (DE3)
-
expression of C-terminally Strep-tagged TenA 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
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)
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67-72
1972
Aneurinibacillus aneurinilyticus, moulds
brenda
Wittliff, J.L.; Airth, R.L.
Thiaminase II (thiamine hydrolase, EC 3.5.99.2)
Methods Enzymol.
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1971
Aneurinibacillus aneurinilyticus, Candida sp. (in: Saccharomycetales), Geotrichum candidum, Trichosporon aneurinolyticum
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brenda
Ikehata, H.
The purification of thiaminase II
J. Gen. Appl. Microbiol.
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1960
Aneurinibacillus aneurinilyticus
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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.
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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 (P25052), Bacillus subtilis
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 (O25874), Helicobacter pylori
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 (P25052), Bacillus subtilis 168 (P25052)
brenda
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