Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1'-methylthiamine + aniline
4-methyl-5-(2-hydroxyethyl)-thiazole + 4-amino-5-(anilinomethyl)-1,2-dimethylpyrimidin-1-ium
-
22% of activity with thiamine
-
-
?
2'-ethylthiamine + aniline
4-methyl-5-(2-hydroxyethyl)-thiazole + 5-(anilinomethyl)-2-ethylpyrimidin-4-amine
-
63% of activity with thiamine
-
-
?
2-(1-hydroxyethyl)thiamine + aniline
4-methyl-2-(1-hydroxyethyl)-5-(2-hydroxyethyl)-thiazole + 5-(anilinomethyl)-2-methylpyrimidin-4-amine
-
92% of activity with thiamine
-
-
?
5-chloroethylthiamine + aniline
4-methyl-5-chloroethyl-thiazole + 5-(anilinomethyl)-2-methylpyrimidin-4-amine
-
67% of activity with thiamine
-
-
?
5-nor-thiamine + aniline
4-methyl-thiazole + 5-(anilinomethyl)-2-methylpyrimidin-4-amine
-
88% of activity with thiamine
-
-
?
O-(beta-D-galactosyl)thiamine + aniline
4-methyl-5-(2-hydroxyethyl-O-beta-D-galactosyl)-thiazole + 5-(anilinomethyl)-2-methylpyrimidin-4-amine
-
63% of activity with thiamine
-
-
?
O-benzoylthiamine + aniline
2-(4-methyl-1,3-thiazol-5-yl)ethyl benzoate + 5-(anilinomethyl)-2-methylpyrimidin-4-amine
-
91% of activity with thiamine
-
-
?
O-S-diacetylthiamine + aniline
1-acetyl-4-methyl-5-(2-hydroxyethyl-O-acetyl)-thiazole + 5-(anilinomethyl)-2-methylpyrimidin-4-amine
-
50% of activity with thiamine
-
-
?
O-succinylthiamine + aniline
4-methyl-5-(2-hydroxyethyl-O-succinyl)-thiazole + 5-(anilinomethyl)-2-methylpyrimidin-4-amine
-
83% of activity with thiamine
-
-
?
pyrithiamine + aniline
2-(2-methylpyridin-3-yl)ethanol + 5-(anilinomethyl)-2-methylpyrimidin-4-amine
-
72% of activity with thiamine
-
-
?
tetrahydrothiamine + aniline
?
-
84% of activity with thiamine
-
-
?
thiamine + 2-aminopyridine
?
-
-
-
-
?
thiamine + 2-hydroxyaniline
4-methyl-5-(2-hydroxyethyl)-thiazole + [(4-amino-2-methylpyrimidin-5-yl)methyl]-N-(2-hydroxyphenyl)amine
-
-
-
-
?
thiamine + 2-mercaptobenzoic acid
?
-
-
-
-
?
thiamine + 2-mercaptoethanol
?
thiamine + 2-methylbenzeneamine
4-methyl-5-(2-hydroxyethyl)-thiazole + [(4-amino-2-methylpyrimidin-5-yl)methyl]-N-(2-methylphenyl)amine
-
i.e. o-toluidine
-
-
?
thiamine + 2-pyridinecarboxylic acid
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-carboxypyridinium
-
i.e. alpha-picolinic acid
-
-
?
thiamine + 3-aminopyridine
?
thiamine + 3-hydroxyaniline
4-methyl-5-(2-hydroxyethyl)-thiazole + [(4-amino-2-methylpyrimidin-5-yl)methyl]-N-(3-hydroxyphenyl)amine
-
-
-
-
?
thiamine + 3-methylbenzeneamine
4-methyl-5-(2-hydroxyethyl)-thiazole + [(4-amino-2-methylpyrimidin-5-yl)methyl]-N-(3-methylphenyl)amine
-
i.e. m-toluidine
-
-
?
thiamine + 3-nitroaniline
?
-
-
-
-
?
thiamine + 3-pyridinecarboxylic acid
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-carboxypyridinium
-
i.e. beta-picolinic acid
-
-
?
thiamine + 4-aminopyridine
?
thiamine + 4-hydroxyaniline
4-methyl-5-(2-hydroxyethyl)-thiazole + [(4-amino-2-methylpyrimidin-5-yl)methyl]-N-(4-hydroxyphenyl)amine
-
-
-
-
?
thiamine + 4-methylbenzeneamine
4-methyl-5-(2-hydroxyethyl)-thiazole + [(4-amino-2-methylpyrimidin-5-yl)methyl]-N-(4-methylphenyl)amine
-
i.e. p-toluidine
-
-
?
thiamine + 4-nitrothiophenolate
4-methyl-5-(2-hydroxyethyl)thiazole + 2-methyl-5[[(4-nitrophenyl)sulfanyl]methyl]pyrimidin-4-amine
no activity with thiaminase II
-
-
?
thiamine + 4-nitrothiophenolate
?
-
-
-
?
thiamine + 4-pyridinecarboxylic acid
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-carboxypyridinium
-
i.e. gamma-picolinic acid
-
-
?
thiamine + 6-aminohexanoic acid
4-methyl-5-(2-hydroxyethyl)-thiazole + 6-[[(4-amino-2-methylpyrimidin-5-yl)methyl]amino]hexanoic acid
-
-
-
-
?
thiamine + adenine
?
-
-
-
-
?
thiamine + alpha-picoline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]alpha-picolinium
-
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
thiamine + beta-picoline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]beta-picolinium
-
-
-
-
?
thiamine + cysteine
?
-
-
-
-
?
thiamine + gamma-picoline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]gamma-picolinium
-
-
-
-
?
thiamine + hydroxyproline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]4-hydroxypyrrolidine-2-carboxylic acid
thiamine + imidazole
4-methyl-5-(2-hydroxyethyl)-thiazole + 5-(1H-imidazol-1-yl-methyl)-2-methylpyrimidin-4-amine
thiamine + L-cysteine
4-methyl-5-(2-hydroxyethyl)-thiazole + 2-[[(4-amino-2-ethylpyrimidin-5-yl)methyl]amino]-3-mercaptopropanoic acid
thiamine + L-lysine
?
-
-
-
-
?
thiamine + m-aminobenzoic acid
4-methyl-5-(2-hydroxyethyl)-thiazole + 3-[[(4-amino-2-methylpyrimidin-5-yl)methyl]amino]benzoic acid
-
-
-
-
?
thiamine + m-phenylene diamine
4-methyl-5-(2-hydroxyethyl)-thiazole + [(4-amino-2-methylpyrimidin-5-yl)methyl]-N-(3-aminophenyl)amine
-
-
-
-
?
thiamine + methylamine
?
-
-
-
-
?
thiamine + nicotinic acid
?
thiamine + o-aminobenzoic acid
4-methyl-5-(2-hydroxyethyl)-thiazole + 2-[[(4-amino-2-methylpyrimidin-5-yl)methyl]amino]benzoic acid
-
-
-
-
?
thiamine + o-phenylene diamine
4-methyl-5-(2-hydroxyethyl)-thiazole + [(4-amino-2-methylpyrimidin-5-yl)methyl]-N-(2-aminophenyl)amine
-
-
-
-
?
thiamine + p-aminobenzoic acid
4-methyl-5-(2-hydroxyethyl)-thiazole + 4-[[(4-amino-2-methylpyrimidin-5-yl)methyl]amino]benzoic acid
-
-
-
-
?
thiamine + p-phenylene diamine
4-methyl-5-(2-hydroxyethyl)-thiazole + [(4-amino-2-methylpyrimidin-5-yl)methyl]-N-(4-aminophenyl)amine
-
-
-
-
?
thiamine + proline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyrrolidine-2-carboxylic acid
thiamine + pyridine
1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
thiamine + pyridine
heteropyrithiamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
thiamine + pyridoxine
?
-
-
-
-
?
thiamine + quinoline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]quinolinium
thiamine + sulfanilamide
?
-
-
-
-
?
thiamine + sulfanilic acid
?
-
-
-
-
?
thiamine + Tris
?
-
-
-
-
?
thiamine + veratrylamine
bis-(4-amino-2-methyl)pyrimidinyl-3,4-dimethoxybenzylamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
the reaction can occur without base substrate
-
?
thiamine disulfide + aniline
?
-
26% of activity with thiamine
-
-
?
thiamine phosphate + aniline
2-(4-methyl-1,3-thiazol-5-yl)ethyl dihydrogenphosphate + 5-(anilinomethyl)-2-methylpyrimidin-4-amine
-
64% of activity with thiamine
-
-
?
thiothiamine + aniline
4-methyl-5-(2-hydroxyethyl)-2-thio-thiazole + 5-(anilinomethyl)-2-methylpyrimidin-4-amine
-
12% of activity with thiamine
-
-
?
additional information
?
-
thiamine
?
-
there is activity without base substrate
-
-
?
thiamine
?
there is degradation of thiamine without a base substrate, possibly the ring-opened form of thiamine functions as the nucleophile
-
-
?
thiamine
?
-
there is activity without base substrate
-
-
?
thiamine + 2-mercaptoethanol
?
-
-
-
-
?
thiamine + 2-mercaptoethanol
?
-
63% of activity with aniline
-
-
?
thiamine + 2-mercaptoethanol
?
-
-
-
-
?
thiamine + 3-aminopyridine
?
-
-
-
-
?
thiamine + 3-aminopyridine
?
-
-
-
-
?
thiamine + 4-aminopyridine
?
-
-
-
-
?
thiamine + 4-aminopyridine
?
-
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
activity found
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
taken as 100% of activity of purified enzyme
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
one molecule of thiamine is cleaved releasing one molecule of methylhydroxyethylthiazole for one molecule of enzyme
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
activity found
-
?
thiamine + aniline
5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + hydroxyproline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]4-hydroxypyrrolidine-2-carboxylic acid
-
-
-
-
?
thiamine + hydroxyproline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]4-hydroxypyrrolidine-2-carboxylic acid
-
-
-
-
?
thiamine + imidazole
4-methyl-5-(2-hydroxyethyl)-thiazole + 5-(1H-imidazol-1-yl-methyl)-2-methylpyrimidin-4-amine
-
24% of activity with aniline
-
-
?
thiamine + imidazole
4-methyl-5-(2-hydroxyethyl)-thiazole + 5-(1H-imidazol-1-yl-methyl)-2-methylpyrimidin-4-amine
-
-
-
-
?
thiamine + L-cysteine
4-methyl-5-(2-hydroxyethyl)-thiazole + 2-[[(4-amino-2-ethylpyrimidin-5-yl)methyl]amino]-3-mercaptopropanoic acid
-
50% of activity with aniline
-
-
?
thiamine + L-cysteine
4-methyl-5-(2-hydroxyethyl)-thiazole + 2-[[(4-amino-2-ethylpyrimidin-5-yl)methyl]amino]-3-mercaptopropanoic acid
-
-
-
-
?
thiamine + nicotinic acid
?
-
-
-
-
?
thiamine + nicotinic acid
?
-
-
-
-
?
thiamine + nicotinic acid
?
-
-
-
-
?
thiamine + proline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyrrolidine-2-carboxylic acid
-
-
-
-
?
thiamine + proline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyrrolidine-2-carboxylic acid
-
-
-
-
?
thiamine + pyridine
1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
-
-
-
?
thiamine + pyridine
1-[(4-amino-2-methylpyrimidin-5-yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole
-
the reaction rate measured by pyridine as the second substrate is three times higher in pI 7-9 enzymes compared with pI 5.7 enzyme
-
-
?
thiamine + pyridine
heteropyrithiamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + pyridine
heteropyrithiamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
best substrate with aniline
-
?
thiamine + pyridine
heteropyrithiamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + pyridine
heteropyrithiamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + pyridine
heteropyrithiamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + pyridine
heteropyrithiamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + pyridine
heteropyrithiamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + pyridine
heteropyrithiamine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
-
-
?
thiamine + quinoline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]quinolinium
-
-
-
-
?
thiamine + quinoline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]quinolinium
-
-
-
-
?
thiamine + quinoline
4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]quinolinium
-
-
-
-
?
additional information
?
-
-
no activity with 4'-deaminothiamine and 4'-oxythiamine suggest that 4'-amino group is essential for enzyme activity
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-Amino-5-(anilinomethyl)-6-chloro-2-methylpyrimidine
-
complete irreversible inhibition 2 times faster than 4-amino-6-chloro-2-methylpyrimidine
4-Amino-6-chloro-2-methylpyrimidine
Ag+
-
100% inhibition at 1 mM
aromatic amines
-
inhibited by or without effect
-
Cd2+
-
the degree of cadmium inhibition, when aniline is the cosubstrate, shows obvious differences between pI isozymes
Dimethialium
-
inactivation at 0.006 mM
heterocyclic amines
-
-
-
thiamine diphosphate
-
inactivation at 0.006 mM
4-Amino-6-chloro-2-methylpyrimidine
-
complete irreversible inhibition, activity protected by thiamine and quinolone
4-Amino-6-chloro-2-methylpyrimidine
inhibitory
4-Amino-6-chloro-2-methylpyrimidine
this suicide substrate is linked to Cys113 of the enzyme
4-aminopyrimidines
-
mostly inhibitory
4-aminopyrimidines
-
mostly inhibitory
aniline
-
highly inhibitory above 2.4 mM
aniline
-
inactivation at 0.006 mM; reactivation at 2 mM
Cu2+
-
different inhibitory effects at 1 mM
Cu2+
-
different inhibitory effects at 1 mM
Cu2+
Celosia crista
-
different inhibitory effects at 1 mM
Cu2+
Dicranopteris sp.
-
different inhibitory effects at 1 mM
Cu2+
-
50% of inhibition at 1 mM
Cu2+
-
different inhibitory effects at 1 mM
Cu2+
-
different inhibitory effects at 1 mM
Fe2+
-
different inhibitory effects at 1 mM
Fe2+
-
different inhibitory effects at 1 mM
Fe2+
Celosia crista
-
different inhibitory effects at 1 mM
Fe2+
Dicranopteris sp.
-
different inhibitory effects at 1 mM
Fe2+
-
70% of inhibition at 1 mM
Fe2+
-
different inhibitory effects at 1 mM
Fe2+
-
different inhibitory effects at 1 mM
Heteropyrithiamine
-
inhibitory at 0.006 mM
Heteropyrithiamine
-
inactivation at 0.006 mM that is restored by pyridine at 25 mM and inhibition of restoration of activity by pyridine at 1 mM
HgCl2
-
potent inhibitor at 0.001 mM
HgCl2
-
potent inhibitor at 0.001 mM
HgCl2
-
potent inhibitor at 0.001 mM
HgCl2
-
potent inhibitor at 0.001 mM
Mersalyl acid
-
potent inhibitor at 0.001 mM
Mersalyl acid
-
potent inhibitor at 0.001 mM
Mersalyl acid
-
potent inhibitor at 0.001 mM
Mersalyl acid
-
potent inhibitor at 0.001 mM
Mn2+
-
different inhibitory effects at 1 mM
Mn2+
-
different inhibitory effects at 1 mM
Mn2+
Celosia crista
-
different inhibitory effects at 1 mM
Mn2+
Dicranopteris sp.
-
different inhibitory effects at 1 mM
Mn2+
-
different inhibitory effects at 1 mM
Mn2+
-
different inhibitory effects at 1 mM
Mn2+
-
different inhibitory effects at 1 mM
p-chloromercuribenzoate
-
complete inhibition at 0.001 mM
p-chloromercuribenzoate
-
complete inhibition at 0.001 mM
p-chloromercuribenzoate
-
50% of inhibition at 0.2 mM and inhibits reactivation by pyridine
p-chloromercuribenzoate
-
complete inhibition at 0.001 mM
p-chloromercuribenzoate
-
complete inhibition at 0.001 mM
thiamine
-
slightly inhibitory above 0.035 mM
thiamine
-
reversible inactivation above 0.0003 mM
thiamine
-
inactivation at 0.006 mM
thiamine
-
inactivation is proportional to thiamine concentration and the thiamine/enzyme ratio is 1 mol/1 mol
additional information
-
not inhibited by EDTA
-
additional information
-
chloramphenicol does not affect activity suggesting that the enzyme has an inactive form
-
additional information
-
primary substrates inactivate the enzyme at 0.006 mM, the lost activity can be restored by incubation at 37°C for 60 min after dialysis or by incubation with secondary substrates or acceptor bases, each substrate at high concentrations abolishes the inactivation of the other substrate
-
additional information
-
acidic conditions prevent inactivation but low pH does not restore activity after inactivation, quaternary nitrogen linked to a substituted pyrimidine ring through a methylene bridge is shared by compounds that inactivates the enzyme, inactivation alters either the net charge or the structure of the protein or both
-
additional information
-
4-amino-2-methyl pyrimidine does not inactivate nor competitively inhibits the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4,5-dimethylthiazole
-
reactivation at 10 mM
5-(2-chloroethyl)-4-methylthiazole
-
reactivation at 10 mM
5-(2-hydroxyethyl)-4-methylthiazole
-
reactivation at 10 mM
cysteine
-
complete reactivation at 3.3 mM but inhibition at 33 mM
Pyridine
-
at 25 mM restores activity inhibited by heteropyrimidine at 0.006 mM
Thioglycollate
-
greater reactivation at 33 mM than at 3.3 mM
thiosulphate
-
greater reactivation at 33 mM than at 3.3 mM
2-mercaptoethanol
-
complete reactivation at 3.3 mM but inhibition at 33 mM
2-mercaptoethanol
-
similar effects as pyridine at 10 mM probably due to its action as secondary substrate
2-mercaptoethanol
-
reactivates enzyme less effectively than dithiothreitol
aniline
Athyrium nipponicum
-
activated by 1 mM
aniline
-
not activated by 1 mM
aniline
-
activated by 1 mM
aniline
-
activated by 1 mM
aniline
-
not activated by 1 mM
aniline
-
activated by 1 mM
aniline
-
reactivation of enzyme at 2 mM
aniline
-
activated by 1 mM
aniline
Polystichum fortunei
-
activated by 1 mM
aniline
-
activated by 1 mM
aniline
-
activated by 1 mM
aniline
-
activated by 1 mM
aromatic amines
-
increased activity, aniline is the most potent activator, primary amines not directly attached to the benzene ring have no effect
-
aromatic amines
Celosia crista
-
increased activity, aniline is the most potent activator, primary amines not directly attached to the benzene ring have no effect
-
aromatic amines
-
increased activity, aniline is the most potent activator, primary amines not directly attached to the benzene ring have no effect
-
aromatic amines
-
increased activity, aniline is the most potent activator, primary amines not directly attached to the benzene ring have no effect
-
aromatic amines
-
increased activity, aniline is the most potent activator, primary amines not directly attached to the benzene ring have no effect
-
dithiothreitol
-
similar effects as pyridine at 10 mM probably due to its action as secondary substrate
dithiothreitol
-
reactivates 60-100% of the original activity
heterocyclic amines
-
pyridine, 2-amino-pyridine, 3-amino-pyridine increase activity
-
heterocyclic amines
-
most 4-aminopyrimidines are inhibitory
-
heterocyclic amines
Celosia crista
-
pyridine, 2-amino-pyridine, 3-amino-pyridine increase activity
-
heterocyclic amines
-
pyridine, 2-amino-pyridine, 3-amino-pyridine increase activity
-
heterocyclic amines
-
most 4-aminopyrimidines are inhibitory
-
heterocyclic amines
-
pyridine, 2-amino-pyridine, 3-amino-pyridine increase activity
-
heterocyclic amines
-
nicotinic acid and quinolone increase activity
-
heterocyclic amines
-
most 4-aminopyrimidines increase activity
-
heterocyclic amines
-
pyridine, 2-amino-pyridine, 3-amino-pyridine increase activity
-
heterocyclic amines
-
nicotinic acid and quinolone increase activity
-
sulfhydryl compounds
-
increase activity, more markedly in bacteria
sulfhydryl compounds
-
increase activity, more markedly in bacteria
sulfhydryl compounds
-
increase activity, more markedly in bacteria
additional information
-
aliphatic amines and taurine have no effect
-
additional information
-
L-phenylalanine, L-tyrosine, L-tryptophan and gamma-aceto-gammachloropropyl acetate have no effect
-
additional information
Celosia crista
-
aliphatic amines and taurine have no effect
-
additional information
-
aliphatic amines and taurine have no effect
-
additional information
-
L-phenylalanine, L-tyrosine, L-tryptophan and gamma-aceto-gammachloropropyl acetate have no effect
-
additional information
-
aliphatic amines and taurine have no effect
-
additional information
-
L-phenylalanine, L-tyrosine, L-tryptophan and gamma-aceto-gammachloropropyl acetate have no effect
-
additional information
-
aliphatic amines and taurine have no effect
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
evolution
-
thiaminase activity is generally higher in the basal teleosts (clupeids, cyprinids, and catostomids) than in the more derived neoteleosts (percids and centrarchids). Thus, thiaminase activity may be a function of trait selection over evolutionary time
malfunction
thiaminase I is specifically implicated in thiamine deficiency syndromes in animals
malfunction
-
thiaminase I is specifically implicated in thiamine deficiency syndromes in animals
-
metabolism
the enzyme cleaves phosphorylated thiamine and toxic analogs, which releases precursors that can then be used for thiamine synthesis
metabolism
-
the enzyme cleaves phosphorylated thiamine and toxic analogs, which releases precursors that can then be used for thiamine synthesis
-
physiological function
-
crucian carp known to harbor thiaminase I activity are injected intramuscularly with live Aeromonas salmonicida. Significantly higher thiaminase activities are measured in all tissues of fish injected with live bacteria than in the control group. Different allocation pattern are shown: The amount of thiaminase I enzyme is elevated in the whole blood of injected fish in the absence of natural cosubstrate(s). The thiaminase activity of the injected, inflamed muscle suggests that both the amount of thiaminase enzyme and an unidentified natural cosubstrate(s) is elevated. This suggests that in addition to the enzyme, some cosubstrate(s) of fish or pathogen origin play a regulatory role in the physiological significance of thiaminase I activity in vivo
physiological function
-
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
physiological function
-
Burkholderia pseudomallei possesses thiaminase I which catalyzes degradation of thiamine to 4-methyl-5-thiazoleethanol. ThiM, which encodes hydroxyethylthiazole kinase responsible for degradation of 4-methyl-5-thiazoleethanol, is absent or not expressed in all Burkholderia pseudomallei strains. The high 4-methyl-5-thiazoleethanol level in Burkholderia pseudomallei is likely due to the absence of hydroxyethylthiazole kinase and hence reduced downstream degradation
physiological function
-
Burkholderia thailandensis possesses thiaminase I which catalyzes degradation of thiamine to 4-methyl-5-thiazoleethanol. ThiM, which encodes hydroxyethylthiazole kinase responsible for degradation of 4-methyl-5-thiazoleethanol, is present and expressed in Burkholderia thailandensis
physiological function
thiaminase I provides a growth advantage by salvaging precursors from environmental thiamine and its analogs in Burkholderia thailandensis
physiological function
-
thiaminase I provides a growth advantage by salvaging precursors from environmental thiamine and its analogs in Burkholderia thailandensis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Fujita, A.
Thiaminase
Adv. Enzymol. Relat. Subj. Biochem.
15
389-421
1954
Acanthogobius flavimanus, Anadara inflata, Anguilla japonica, Athyrium nipponicum, Auxis hira, Aneurinibacillus aneurinilyticus, Paenibacillus thiaminolyticus, Turbo cornutus, Struthiopteris nipponica, Carassius auratus, Cyprinus carpio, Celosia crista, Charybdis 6-dentata, Circe scripta, Clava kochi, Corbicula leana, Cristaria plicata, Dicranopteris linearis, Dicranopteris sp., Dryopteris erythrosora, Dryopteris lacera, Eleotris oxycephala, Equisetum arvense, Eviota abax, Gnathopogon mayedae, Haliotis gigantea, Haliotis japonica, Hypomesus olidus, Ischikauia steenackeri, Leucopsarion petersii, Lycopodium clavatum, Mactra sulcataria, Mactra quadrangularis, 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, Panulirus japonicus, Paphia philippinarum, Silurus asotus, Leptochilus ellipticus, Polystichum aculeatum, Polystichum falcatum, Polystichum fortunei, Polystichum tsus-simense, Portunus trituberculatus, Pteridium aquilinum, Rhinogobius similis, Solen gouldi, Thiara libertina, Umbonium costatum, Viviparus malleatus, Aneurinibacillus aneurinilyticus BKA, Paenibacillus thiaminolyticus BMM
brenda
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
brenda
Boyd, J.W.
Studies on thiaminase I activity in ruminant faeces and rumen bacteria
J. Agric. Sci.
104
637-642
1985
Megasphaera elsdenii
-
brenda
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
brenda
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
brenda
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
brenda
McCleary, B.V.; Chick, B.F.
The purification and properties of a thiaminase I enzyme from nardoo (Marsilea Drumondii)
Phytochemistry
16
207-213
1977
Cheilanthes sieberi, Marsilea angustifolia, Marsilea drummondii, Marsilea mutica, Pteridium esculentum, Velesunio ambiguus
-
brenda
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
brenda
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
brenda
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)
brenda
Fabre, B.; Geay, B.; Beaufils, P.
Thiaminase activity in Equisetum arvense and its extracts
Plant. Med. Phytother.
26
190-197
1993
Equisetum arvense
-
brenda
Sato, M.; Hayashi, S.; Nishino, K.
Subcellular localization of thiaminase I in the kidney and spleen of carp, Cyprinus carpio
Comp. Biochem. Physiol. A
108A
31-38
1994
Cyprinus carpio
-
brenda
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
-
brenda
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
brenda
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)
-
brenda
Bos, M.; Kozik, A.
Some molecular and enzymatic properties of a homogeneous preparation of thiaminase I purified from carp liver
J. Protein Chem.
19
75-84
2000
Cyprinus carpio
brenda
Wistbacka, S.; Heinonen, A.; Bylund, G.
Thiaminase activity of gastrointestinal contents of salmon and herring from the Baltic Sea
J. Fish Biol.
60
1031-1042
2002
Clupea harengus, Salmo salar
-
brenda
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, Paenibacillus thiaminolyticus (P45741)
brenda
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)
brenda
Wistbacka, S.; Bylund, G.
Thiaminase activity of Baltic salmon prey species: a comparison of net- and predator-caught samples
J. Fish Biol.
72
787-802
2008
Clupea harengus, Sprattus sprattus, Gasterosteus aculeatus
-
brenda
Nishimune, T.; Watanabe, Y.; Okazaki, H.
Studies on the polymorphism of thiaminase I in seawater fish
J. Nutr. Sci. Vitaminol.
54
339-346
2008
Fistularia petimba
brenda
Wistbacka, S.; Loennstroem, L.G.; Bonsdorff, E.; Bylund, G.
Thiaminase activity of crucian carp Carassius carassius injected with a bacterial fish pathogen, Aeromonas salmonicida subsp. salmonicida
J. Aquat. Anim. Health
21
217-228
2009
Carassius carassius
brenda
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
brenda
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
brenda
Sikowitz, M.D.; Shome, B.; Zhang, Y.; Begley, T.P.; Ealick, S.E.
Structure of a Clostridium botulinum C143S thiaminase I/thiamin complex reveals active site architecture
Biochemistry
52
7830-7839
2013
Clostridium botulinum
brenda
Lau, S.; Lam, C.; Curreem, S.; Lee, K.; Chow, W.; Lau, C.; Sridhar, S.; Wong, S.; Martelli, P.; Hui, S.; Yuen, K.; Woo, P.
Metabolomic profiling of Burkholderia pseudomallei using UHPLC-ESI-Q-TOF-MS reveals specific biomarkers including 4-methyl-5-thiazoleethanol and unique thiamine degradation pathway
Cell Biosci.
5
26
2015
Burkholderia pseudomallei, Burkholderia thailandensis
brenda
Blakeslee, C.; Sweet, S.; Galbraith, H.; Honeyfield, D.
Thiaminase activity in native freshwater mussels
J. Great Lakes Res.
41
516-519
2015
Strophitus undulatus, Elliptio complanata
-
brenda
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
brenda
Sannino, D.R.; Kraft, C.E.; Edwards, K.A.; Angert, E.R.
Thiaminase I provides a growth advantage by salvaging precursors from environmental thiamine and its analogs in Burkholderia thailandensis
Appl. Environ. Microbiol.
84
e01268-18
2018
Burkholderia thailandensis (Q2T5P7), Burkholderia thailandensis, Burkholderia thailandensis ATCC 700388 (Q2T5P7)
brenda
Boggs, K.; Spooner, D.; Honeyfield, D.; Shull, D.; Wertz, T.; Sweet, S.
Phylogeny and foraging mode correspond with thiaminase activity in freshwater fishes Potential links to environmental factors
Freshw. Sci.
38
605-615
2019
Notropis hudsonius, Catostomus commersonii, Alosa pseudoharengus, Fundulus diaphanus, Campostoma anomalum, Luxilus cornutus, Exoglossum maxillingua, Semotilus corporalis, Rhinichthys cataractae, Etheostoma olmstedi, Dorosoma cepedianum
-
brenda