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Information on EC 2.5.1.2 - thiamine pyridinylase and Organism(s) Paenibacillus thiaminolyticus and UniProt Accession P45741

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IUBMB Comments
Various bases and thiol compounds can act instead of pyridine.
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Select one or more organisms in this record:
This record set is specific for:
Paenibacillus thiaminolyticus
UNIPROT: P45741
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Paenibacillus thiaminolyticus
Synonyms
pyrimidine transferase, thiamin hydrolase, thiamin pyridinolase, thiamin pyridinylase, thiaminase, thiaminase I, thiamine pyridinolase, thiamine pyridinylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pyrimidine transferase
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-
-
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thiamin hydrolase
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-
-
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thiamin pyridinolase
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thiamin pyridinylase
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-
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thiaminase
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-
-
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thiaminase I
thiamine pyridinolase
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thiamine pyridinylase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pyrimidyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
thiamine:base 2-methyl-4-aminopyrimidine-5-methenyltransferase
Various bases and thiol compounds can act instead of pyridine.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-35-7
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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
thiamine
?
show the reaction diagram
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there is degradation of thiamine without a base substrate, possibly the ring-opened form of thiamine functions as the nucleophile
-
-
?
thiamine + 4-nitrothiophenolate
4-methyl-5-(2-hydroxyethyl)thiazole + 2-methyl-5[[(4-nitrophenyl)sulfanyl]methyl]pyrimidin-4-amine
show the reaction diagram
no activity with thiaminase II
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-
?
thiamine + veratrylamine
bis-(4-amino-2-methyl)pyrimidinyl-3,4-dimethoxybenzylamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
show the reaction diagram
the reaction can occur without base substrate
-
?
thiamine + 4-nitrothiophenolate
?
show the reaction diagram
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
show the reaction diagram
thiamine + pyridine
heteropyrithiamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
show the reaction diagram
thiamine + quinoline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]quinolinium
show the reaction diagram
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-
-
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?
additional information
?
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primary substrates inactivate the enzyme at 0.006 mM and secondary substrates or acceptor bases reactivate the enzyme at 10 mM, each substrate at high concentrations eliminates the inactivation of the other substrate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Amino-6-chloro-2-methylpyrimidine
4-Amino-5-(anilinomethyl)-6-chloro-2-methylpyrimidine
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complete irreversible inhibition 2 times faster than 4-amino-6-chloro-2-methylpyrimidine
4-Amino-6-chloro-2-methylpyrimidine
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complete irreversible inhibition, activity protected by thiamine and quinolone
aniline
Cu2+
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no inhibition
Dimethialium
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inactivation at 0.006 mM
Fe2+
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no inhibition
Heteropyrithiamine
Mn2+
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different inhibitory effects at 1 mM
p-chloromercuribenzoate
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50% of inhibition at 0.2 mM and inhibits reactivation by pyridine
thiamine
thiamine diphosphate
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inactivation at 0.006 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
4,5-dimethylthiazole
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reactivation at 10 mM
5-(2-chloroethyl)-4-methylthiazole
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reactivation at 10 mM
5-(2-hydroxyethyl)-4-methylthiazole
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reactivation at 10 mM
aniline
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reactivation of enzyme at 2 mM
aromatic amines
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increased activity, aniline is the most potent activator, primary amines not directly attached to the benzene ring have no effect
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dithiothreitol
heterocyclic amines
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most 4-aminopyrimidines increase activity; nicotinic acid and quinolone increase activity; pyridine, 2-amino-pyridine, 3-amino-pyridine increase activity
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Pyridine
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at 25 mM restores activity inhibited by heteropyrimidine at 0.006 mM
sulfhydryl compounds
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increase activity, more markedly in bacteria
additional information
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aliphatic amines and taurine have no effect; L-phenylalanine, L-tyrosine, L-tryptophan and gamma-aceto-gammachloropropyl acetate have no effect
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0364
4-nitrothiophenolate
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0.0037 - 0.0211
thiamine
0.0364
4-nitrothiophenolate
pH 7.2, temperature not specified in the publication
2.9
aniline
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pH 5.8, 25°C, the enzyme does not follow strict Michaelis-Menten kinetics
0.0087 - 0.0211
thiamine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
297
4-nitrothiophenolate
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297
4-nitrothiophenolate
pH 7.2, temperature not specified in the publication
260
thiamine
pH 7.2, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8380
4-nitrothiophenolate
pH 7.2, temperature not specified in the publication
12400
thiamine
pH 7.2, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.7
4-Amino-6-chloro-2-methylpyrimidine
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-
0.096
4-Amino-5-(anilinomethyl)-6-chloro-2-methylpyrimidine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 6.8
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assay at 25ºC
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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in 50 mM sodium phosphate at pH 7
37
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in 0.1 M sodium phosphate buffer at pH 5.8
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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more than 90% of activity remains after 20 min
65
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activity abolished after 20 min
100
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inactivation after 20 min
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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although thiaminase I exposure does not stimulate the energy-sensing signaling kinases AKT, AMPK and GSK-3beta in MCF-7, ZR75, HS-578T and T-47D cell lines, thiaminase I exposure does stimulate expression of the ER stress response protein GRP78. Thiaminase I is cytotoxic in breast cancer cell lines and triggers the unfolded protein response
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
THI1_PANTH
409
1
45214
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
-
sedimentation and diffusion data
additional information
a comparison of thiamin-binding protein tbpA from Escherichia coli and thiaminase-I, reveals structural similarity between the two proteins, specially in domain 1, suggesting that the two proteins evolve from a common ancestor
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
by vapour-diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C113S
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inactive mutant at the active nucleophilic site
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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50 mM sodium phosphate buffer, 2 mM dithiothreitol, 2 mM EDTA
636853, 636858
5.8
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0.1 M sodium phosphate buffer
636846, 636850
6.5
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0.15 M citrate-phosphate buffer
636849
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of dithiothreitol, 2 mM, reduces the loss of activity
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636853
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
by ammonium precipitation, DEAE column, Cibacron blue dye affinity column
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ammonium precipitation and gel filtration
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by ammonium precipitation, Sephadex G-25 column, Sephadex G-100 column and DEAE-Sephadex column
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HisTrap FF column chromatography
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Tris-glycine polyacrylamide electrophoresis
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli with Gly6 changed to Ala6 with no apparent effect
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expressed in Escherichia coli BL21(DE3) cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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improvements in a spectrophotometric thiaminase I activity assay that measures the disappearance of 4-nitrothiophenol providing scalable sample processing protocols and a 96-well microtiter plate format. Organisms devoid of thiaminase I, based upon previous work, show no activity with this assay. In addition, activity is found in a variety of fishes and one fern species from which this enzyme has not previously been reported
medicine
nutrition
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thiaminase can be used as an effective method for thiamine determination in food and fodder
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujita, A.
Thiaminase
Adv. Enzymol. Relat. Subj. Biochem.
15
389-421
1954
Acanthogobius flavimanus, Anadara inflata, Aneurinibacillus aneurinilyticus, Aneurinibacillus aneurinilyticus BKA, Anguilla japonica, Athyrium nipponicum, Auxis hira, Carassius auratus, Celosia crista, Charybdis 6-dentata, Circe scripta, Clava kochi, Corbicula leana, Cristaria plicata, Cyprinus carpio, Dicranopteris linearis, Dicranopteris sp., Dryopteris erythrosora, Dryopteris lacera, Eleotris oxycephala, Equisetum arvense, Eviota abax, Gnathopogon mayedae, Haliotis gigantea, Haliotis japonica, Hypomesus olidus, Ischikauia steenackeri, Leptochilus ellipticus, Leucopsarion petersii, Lycopodium clavatum, Mactra quadrangularis, Mactra sulcataria, Meretrix meretrix, Misgurnus anguillicaudatus, Mugil cephalus, no activity in Astroconger myriaster, no activity in Cambaroides japonicus, no activity in Camposcia retusa, no activity in Metapenaeopsis acclivis, no activity in Plecoglossus altivelis, no activity in Squilla oratoria, Odontobutis obscura, Osmunda japonica, Ostrea laperousei, Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus BMM, Panulirus japonicus, Paphia philippinarum, Polystichum aculeatum, Polystichum falcatum, Polystichum fortunei, Polystichum tsus-simense, Portunus trituberculatus, Pteridium aquilinum, Rhinogobius similis, Silurus asotus, Solen gouldi, Struthiopteris niponica, Thiara libertina, Turbo cornutus, Umbonium costatum, Viviparus malleatus
Manually annotated by BRENDA team
Wittliff, J.L.; Airth, R.L.
The extracellular thiaminase I of Bacillus thiaminolyticus. I. Purification and physicochemical properties
Biochemistry
7
736-744
1968
Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus M
Manually annotated by BRENDA team
Suzuki, K.; Ooba, J.I.
Reversible inactivation of cellular thiaminase I in Bacillus thiaminolyticus by thiamine and heteropyrithiamine
J. Biochem.
72
1053-1055
1972
Paenibacillus thiaminolyticus
Manually annotated by BRENDA team
Suzuki, K.; Ooba, J.I.
Reversible inactivation of extracellular thiaminase I in Bacillus thiaminolyticus. I. Inactivation by the primary substrate and reactivation by the secondary substrate
Biochim. Biophys. Acta
293
111-117
1973
Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus YUSM I00I
Manually annotated by BRENDA team
Agee, C.C.; Airth, R.L.
Reversible inactivation of thiaminase I of Bacillus thiaminolyticus by its primary substrate, thiamine
J. Bacteriol.
115
957-965
1973
Paenibacillus thiaminolyticus
Manually annotated by BRENDA team
Hutter, J.A.; Slama, J.T.
Inhibition of thiaminase I from Bacillus thiaminolyticus. Evidence supporting a covalent 1,6-dihydropyrimidinyl-enzyme intermediate
Biochemistry
26
1969-1973
1987
Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus BMM
Manually annotated by BRENDA team
Costello, C.A.; Kelleher, N.L.; Abe, M.; McLafferty, F.W.; Begley, T.P.
Mechanistic studies on thiaminase I. Overexpression and identification of the active site nucleophile
J. Biol. Chem.
271
3445-3452
1996
Paenibacillus thiaminolyticus (P45741), Paenibacillus thiaminolyticus
Manually annotated by BRENDA team
Kelleher, N.L.; Nicewonger, R.B.; Begley, A.P.; McLafferty, F.W.
Identification of modification sites in large biomolecules by stable isotope labeling and tandem high resolution mass spectrometry. The active site nucleophile of thiaminase I
J. Biol. Chem.
272
32215-32220
1997
Paenibacillus thiaminolyticus (P45741)
Manually annotated by BRENDA team
Ruml, T.; Silhankova, L.; Brunerova, M.
Purification of thiaminase I for analytical purposes
Potravinarske Vedy
13
181-187
1995
Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus DBM 1068
-
Manually annotated by BRENDA team
Campobasso, N.; Begun, J.; Costello, C.A.; Begley, T.P.; Ealick, S.E.
Crystallization and preliminary x-ray analysis of thiaminase I from Bacillus thiaminolyticus: space group change upon freezing of crystals
Acta Crystallogr. Sect. D
54
448-450
1998
Paenibacillus thiaminolyticus (P45741), Paenibacillus thiaminolyticus
Manually annotated by BRENDA team
Wu, M.; Papish, E.T.; Begley, T.P.
Mechanistic studies on thiaminase I. Identification of the product of thiamin degradation in the absence of the nucleophilic cosubstrate
Bioorg. Chem.
28
45-48
2000
Paenibacillus thiaminolyticus (P45741)
-
Manually annotated by BRENDA team
Hanes, J.W.; Kraft, C.E.; Begley, T.P.
An assay for thiaminase I in complex biological samples
Anal. Biochem.
368
33-38
2007
Paenibacillus thiaminolyticus (P45741), Paenibacillus thiaminolyticus
Manually annotated by BRENDA team
Soriano, E.V.; Rajashankar, K.R.; Hanes, J.W.; Bale, S.; Begley, T.P.; Ealick, S.E.
Structural similarities between thiamin-binding protein and thiaminase-I suggest a common ancestor
Biochemistry
47
1346-1357
2008
Paenibacillus thiaminolyticus (P45741)
Manually annotated by BRENDA team
Liu, S.; Monks, N.R.; Hanes, J.W.; Begley, T.P.; Yu, H.; Moscow, J.A.
Sensitivity of breast cancer cell lines to recombinant thiaminase I
Cancer Chemother. Pharmacol.
66
171-179
2010
Paenibacillus thiaminolyticus
Manually annotated by BRENDA team
Liu, S.; Bae, Y.; Leggas, M.; Daily, A.; Bhatnagar, S.; Miriyala, S.; St Clair, D.K.; Moscow, J.A.
Pharmacologic properties of polyethylene glycol-modified Bacillus thiaminolyticus thiaminase I enzyme
J. Pharmacol. Exp. Ther.
341
775-783
2012
Paenibacillus thiaminolyticus
Manually annotated by BRENDA team
Kraft, C.; Gordon, E.; Angert, E.
A rapid method for assaying thiaminase I activity in diverse biological samples
PLoS ONE
9
e92688
2014
Paenibacillus thiaminolyticus, Paenibacillus thiaminolyticus 8103
Manually annotated by BRENDA team
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