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(R)-(-)-1-amino-2-propanol + NAD+
?
acetoin + NAD+
butan-2,3-dione + NADH + H+
butane-2,3-diol + NAD+
? + NADH
-
-
-
-
?
citric acid + NAD+
?
low activity
-
-
?
D-allothreonine + NAD+
D-2-amino-3-oxobutanoate + NADH
-
-
-
?
D-glucose + NAD+
?
-
-
-
?
D-threonine + NAD+
(2R)-2-amino-3-oxobutanoate + NADH + H+
lowest activity
-
-
?
D-threonine + NAD+
D-2-amino-3-oxobutyrate + NADH
-
-
-
-
?
DL-2-amino-3-hydroxypentanoate + NAD+
L-2-amino-3-oxopentanoate + NADH
DL-2-amino-3-hydroxyvalerate + NAD+
DL-2-amino-3-oxopentanoate + NADH + H+
DL-2-amino-3-hydroxyvalerate + NAD+
DL-2-amino-3-oxovalerate + NADH
DL-3-hydroxynorvaline + NAD+
3-oxonorvaline + NADH + H+
DL-allothreonine + NAD+
D-2-amino-3-oxobutanoate + NADH
-
-
-
?
DL-threo-3-hydroxynorvaline + NAD+
? + NADH
DL-threo-3-phenylserine + NAD+
? + NADH
DL-threo-beta-phenylserine + NAD+
DL-2-amino-3-phenyl-3-oxopropionate + NADH
DL-threonine hydroxamate + NAD+
DL-2-amino-3-oxobutoxamate + NADH
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
high activity
-
-
?
glycerol + NAD+
?
-
-
-
?
isopropanol + NAD+
isopropylaldehyde + NADH + H+
-
-
-
?
L-allothreonine + NAD+
L-2-amino-3-oxobutanoate + NADH
-
-
-
?
L-serine + NAD+
3-oxo-L-alanine + NADH + H+
-
-
-
?
L-serine + NAD+
L-2-amino-3-oxopropionate + NADH + H+
L-threonine + 3-acetyl-pyridine adenine dinucleotide
L-2-amino-3-oxobutanoate + ?
L-threonine + 3-pyridinealdehyde adenine dinucleotide
L-2-amino-3-oxobutanoate + ?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
L-threonine + NAD+
L-2-amino-3-oxobutanoate + NADH + H+
L-threonine + nicotinamide guanine dinucleotide
L-2-amino-3-oxobutanoate + ?
5.1% the rate of NAD+
-
-
?
L-threonine + thionicotinamide-NAD+
L-2-amino-3-oxobutanoate + ?
5.1% the rate of NAD+
-
-
?
L-threonine amide + NAD+
L-2-amino-3-oxobutyramide + NADH
L-threonine methyl ester + NAD+
L-2-amino-3-oxobutanoate methyl ester + NADH
lactic acid + NAD+
?
low activity
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
low activity
-
-
?
n-butanol + NAD+
butanal + NADH + H+
highest activity
-
-
?
additional information
?
-
(R)-(-)-1-amino-2-propanol + NAD+
?
activity with mutant enzyme G114A. No activity with wild-type enzyme
-
-
?
(R)-(-)-1-amino-2-propanol + NAD+
?
activity with mutant enzyme G114A. No activity with wild-type enzyme
-
-
?
acetoin + NAD+
butan-2,3-dione + NADH + H+
1% of the activity compared to L-threonine
-
-
?
acetoin + NAD+
butan-2,3-dione + NADH + H+
1% of the activity compared to L-threonine
-
-
?
DL-2-amino-3-hydroxypentanoate + NAD+
L-2-amino-3-oxopentanoate + NADH
-
-
-
?
DL-2-amino-3-hydroxypentanoate + NAD+
L-2-amino-3-oxopentanoate + NADH
-
-
-
?
DL-2-amino-3-hydroxyvalerate + NAD+
DL-2-amino-3-oxopentanoate + NADH + H+
-
-
-
?
DL-2-amino-3-hydroxyvalerate + NAD+
DL-2-amino-3-oxopentanoate + NADH + H+
-
-
-
?
DL-2-amino-3-hydroxyvalerate + NAD+
DL-2-amino-3-oxovalerate + NADH
-
-
-
?
DL-2-amino-3-hydroxyvalerate + NAD+
DL-2-amino-3-oxovalerate + NADH
-
-
-
?
DL-3-hydroxynorvaline + NAD+
3-oxonorvaline + NADH + H+
20% of the activity compared to L-threonine
-
-
?
DL-3-hydroxynorvaline + NAD+
3-oxonorvaline + NADH + H+
20% of the activity compared to L-threonine
-
-
?
DL-threo-3-hydroxynorvaline + NAD+
? + NADH
31% the rate of L-threonine
-
-
?
DL-threo-3-hydroxynorvaline + NAD+
? + NADH
31% the rate of L-threonine
-
-
?
DL-threo-3-phenylserine + NAD+
? + NADH
-
53% of the activity with L-threonine
-
-
?
DL-threo-3-phenylserine + NAD+
? + NADH
-
53% of the activity with L-threonine
-
-
?
DL-threo-beta-phenylserine + NAD+
DL-2-amino-3-phenyl-3-oxopropionate + NADH
-
-
-
?
DL-threo-beta-phenylserine + NAD+
DL-2-amino-3-phenyl-3-oxopropionate + NADH
-
-
-
?
DL-threo-beta-phenylserine + NAD+
DL-2-amino-3-phenyl-3-oxopropionate + NADH
-
-
-
?
L-serine + NAD+
? + NADH
-
-
-
-
?
L-serine + NAD+
? + NADH
-
21% of the activity with L-threonine
-
-
?
L-serine + NAD+
? + NADH
-
21% of the activity with L-threonine
-
-
?
L-serine + NAD+
L-2-amino-3-oxopropionate + NADH + H+
-
-
-
?
L-serine + NAD+
L-2-amino-3-oxopropionate + NADH + H+
-
-
-
?
L-serine + NAD+
L-2-amino-3-oxopropionate + NADH + H+
-
-
-
?
L-serine + NAD+
L-2-amino-3-oxopropionate + NADH + H+
-
-
-
-
?
L-serine + NAD+
L-2-amino-3-oxopropionate + NADH + H+
-
-
-
?
L-serine + NAD+
L-2-amino-3-oxopropionate + NADH + H+
-
-
-
?
L-threonine + 3-acetyl-pyridine adenine dinucleotide
L-2-amino-3-oxobutanoate + ?
60.6% the rate of NAD+
-
-
?
L-threonine + 3-acetyl-pyridine adenine dinucleotide
L-2-amino-3-oxobutanoate + ?
60.6% the rate of NAD+
-
-
?
L-threonine + 3-pyridinealdehyde adenine dinucleotide
L-2-amino-3-oxobutanoate + ?
7.2% the rate of NAD+
-
-
?
L-threonine + 3-pyridinealdehyde adenine dinucleotide
L-2-amino-3-oxobutanoate + ?
7.2% the rate of NAD+
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
high activity
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
r
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
substrate binding involved residues G66, G71, G77, and V80, H94 is an active site residue
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
r
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
stereospecificity, overview
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
active site structure, overview
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
stereospecificity, overview
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
catabolism through the threonine dehydrogenase pathway does not account for the high first-pass extraction rate of dietary threonine by the portal drained viscera in pigs, overview
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
?
L-threonine + NAD+
L-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
L-2-amino-3-oxobutanoate + NADH + H+
the product L-2-amino-3-oxobutanoate is unstable. It spontaneously converts to 2,5-dimethylpyrazine in a pH-dependent reaction, via 3,6-dihydro-2,5-dimethylpyrazine. The reaction from aminoacetone to 2,5-dimethylpyrazine is a pH-dependent nonenzymatic reaction. Inactivation of 2-amino-3-ketobutyrate coenzyme A ligase in Bacilus subtilis improves 2,5-dimethylpyrazine production
-
-
?
L-threonine + NAD+
L-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
L-2-amino-3-oxobutanoate + NADH + H+
the product L-2-amino-3-oxobutanoate is unstable. It spontaneously converts to 2,5-dimethylpyrazine in a pH-dependent reaction, via 3,6-dihydro-2,5-dimethylpyrazine. The reaction from aminoacetone to 2,5-dimethylpyrazine is a pH-dependent nonenzymatic reaction. Inactivation of 2-amino-3-ketobutyrate coenzyme A ligase in Bacilus subtilis improves 2,5-dimethylpyrazine production
-
-
?
L-threonine + NAD+
L-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
L-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine + NAD+
L-2-amino-3-oxobutanoate + NADH + H+
-
-
-
?
L-threonine amide + NAD+
L-2-amino-3-oxobutyramide + NADH
-
-
-
?
L-threonine amide + NAD+
L-2-amino-3-oxobutyramide + NADH
-
-
-
?
L-threonine amide + NAD+
L-2-amino-3-oxobutyramide + NADH
-
-
-
?
L-threonine methyl ester + NAD+
L-2-amino-3-oxobutanoate methyl ester + NADH
-
-
-
?
L-threonine methyl ester + NAD+
L-2-amino-3-oxobutanoate methyl ester + NADH
-
-
-
?
L-threonine methyl ester + NAD+
L-2-amino-3-oxobutanoate methyl ester + NADH
-
-
-
?
L-threoninol + NAD+
?
-
-
-
?
L-threoninol + NAD+
?
-
-
-
?
additional information
?
-
no activity with L-theronine methyl ester, L-threonine amide, DL-threonine hydroxamate, L-homoserine, (R)-1-amino-2-propanol, L-malate, (R)-3-hydroxybutyrate, DL-threo-phenylserine, L-serine
-
-
?
additional information
?
-
-
no activity with L-theronine methyl ester, L-threonine amide, DL-threonine hydroxamate, L-homoserine, (R)-1-amino-2-propanol, L-malate, (R)-3-hydroxybutyrate, DL-threo-phenylserine, L-serine
-
-
?
additional information
?
-
no activity with L-theronine methyl ester, L-threonine amide, DL-threonine hydroxamate, L-homoserine, (R)-1-amino-2-propanol, L-malate, (R)-3-hydroxybutyrate, DL-threo-phenylserine, L-serine
-
-
?
additional information
?
-
L-threonine and DL-2-amino-3-hydroxyvalerate are the only substrates for ThrDH among other L-amino acids, alcohols, and amino alcohols, substrate specificity, overview
-
-
?
additional information
?
-
-
L-threonine and DL-2-amino-3-hydroxyvalerate are the only substrates for ThrDH among other L-amino acids, alcohols, and amino alcohols, substrate specificity, overview
-
-
?
additional information
?
-
L-threonine and DL-2-amino-3-hydroxyvalerate are the only substrates for ThrDH among other L-amino acids, alcohols, and amino alcohols, substrate specificity, overview
-
-
?
additional information
?
-
-
L-threonine and DL-2-amino-3-hydroxyvalerate are the only substrates for ThrDH among other L-amino acids, alcohols, and amino alcohols, substrate specificity, overview
-
-
?
additional information
?
-
specific for L-form of threonine, no substrate: NADP, nicotinic acid adenine dinucleotide, alpha-NAD, nicotinamide hypoxanthine dinucleotide
-
-
?
additional information
?
-
-
specific for L-form of threonine, no substrate: NADP, nicotinic acid adenine dinucleotide, alpha-NAD, nicotinamide hypoxanthine dinucleotide
-
-
?
additional information
?
-
specific for L-form of threonine, no substrate: NADP, nicotinic acid adenine dinucleotide, alpha-NAD, nicotinamide hypoxanthine dinucleotide
-
-
?
additional information
?
-
-
broad substrate specificity, determinants, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme is an NAD+-dependent zinc-containing medium-chain enzyme
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
ste11 gene encoding a TDH may function as a modifier gene of ebosin during its biosynthesis
-
-
?
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1,10-phenanthroline
-
1.26 mM, 41% inhibition after 1 h, 82% inhibition after 2 h, no change in remaining activity after removal of 1,10-phenanthroline
4-chloromercuribenzonic acid
94% inhibition at 10 mM
5,5'-dithiobis-(2-nitrobenzoic acid)
-
0.25 mM, 90% inhibition, 67% activity is recovered after incubation with 1 mM, 2-mercaptoethanol or dithieothreitol for 15 min
adenosine-5'-diphosphoribose
aminoacetone
-
uncompetitive inhibition vs. NAD+ or L-threonine
Be2+
-
3.2 mM, 20-50% inhibition
calcium pantothenate
slight inhibition
Cd2+
-
0.05 and 1.0 mM, 90% inhibition
Co2+
0.9 mM, 61% inhibiton
CuCl2
1 mM, 100% inhibition
dipicolinic acid
-
40 mM, 99% inhibition after 1 h, complete loss of enzyme-bound Zn2+
FeCl2
32% inhibition at 1 mM after 60 min
FeCl3
73% inhibition at 1 mM after 60 min
HCO3-
-
noncompetitive inhibition vs. NAD+ or L-threonine
iodoacetic acid
52% inhibition at 10 mM
Iodosobenzoic acid
-
0.3 mM, 17% inhibition
K3[Fe(CN)6]
25% inhibition at 10 mM
L-2-amino-3-oxobutyrate
-
competitive product inhibition by the unstable L-2-amino-3-oxobutyrate only in presence of NADH, which stabilizes
methyl p-nitrobenzenesulfonate
-
2 mM, 40% inhibition within 80 min, 65% protection with 250 mM L-threonine, 64% with 250 mM L-threonine methyl ester, 58% with 250 mM L-threonine amide
methylglyoxal
-
1.0 mM, 42% inhibition, 2 mM, 63% inhibition, methylglyoxal binds at an allosteric site of the enzyme
methylmethanethiosulfonate
-
0.4 mM, 350fold molar excess over enzyme sulfhydryl groups leads to complete inactivation
monoiodoacetate
10 mM, 100% inhibition
NAD+
-
competitive inhibition of L-2-amino-3-oxobutanoate reduction
NaN3
88% inhibition at 10 mM
p-chloromercuribenzoate
-
complete inhibition
p-chloromercuribenzoic acid
10 mM, 44% inhibition
phenazinemethosulfate
complete inhibition
phenylmethanesulfonyl fluoride
63% inhibition at 10 mM
SnCl2
16% inhibition at 1 mM after 60 min
thionitrobenzoate
-
40fold molar excess, gradual 99% loss of enzyme activity
ZnCl2
1 mM, 72% inhibition
adenosine-5'-diphosphoribose
-
adenosine-5'-diphosphoribose
-
competive inhibition vs. NAD+, noncompetitive inhibition vs. L-threonine
Ag+
-
-
Ag+
-
0.064 mM, activity is completely blocked
Cu2+
0.9 mM, 54% inhibiton
Cu2+
-
3.2 mM, 20-50% inhibition
Cu2+
-
3.2 mM, 67% inhibition
Cu2+
-
0.05 and 1.0 mM, 90% inhibition
EDTA
-
-
EDTA
-
50 mM, 99% inhibition after 1 h, complete loss of enzyme-bound Zn2+
EDTA
-
complete inhibition, fully reversible by Zn2+ or Co2+
EDTA
-
complete inhibition at 50 mM
EDTA
-
retains 65% of its original activity after dialysis at 48°C against a buffer containing 1 mM EDTA. Activity is lost when TDH is heated at 60°C for 40 min and in boiling water for 5 min in the presence of 1 mM EDTA
Hg2+
-
-
Hg2+
-
0.5 mM, 100% inhibition of wild-type and C38D mutant enzyme
Hg2+
-
0.064 mM, activity is completely blocked
Hg2+
-
0.25 mM, complete inhibition, 0.05 mM, 95% inhibition
HgCl2
77% inhibition at 1 mM after 60 min
HgCl2
10 mM, 100% inhibition
iodoacetamide
99% inhibition at 10 mM
iodoacetamide
-
3.2 mM, 10% inhibition
iodoacetamide
-
30 mM, 15% inhibition
iodoacetate
-
iodoacetate reacts with 1 sulfhydryl group per subunit of the enzyme, enzyme retains 15% of its initial activity
iodoacetate
-
15% protection against inhibition with 5 mM NAD+, 30% with 5 mM L-threonine, 60-70% protection in the presence of both NAD+ and L-threonine, inactivation occurs more rapidly in the presence of Cd2+; enzyme contains 6 half-cystine residues per subunit, 2 disulfide bonds and 4 sulfhydryl groups
Mn2+
-
preincubation with 1 mM, 47% inhibition of L-threonine amide oxidation, 73% inhibition of L-threonine methyl ester oxidation, 59% inhibition of L-serine oxidation, 48% inhibition of D,L-threo-beta-phenylserine oxidation
Mn2+
-
1.0 mM, 40-50% inhibition
N-ethylmaleimide
complete inhibition
N-ethylmaleimide
10 mM, 48% inhibition
N-ethylmaleimide
-
0.32 mM, 10 min, 37°C, 23% inhibition
NADH
competitive to NAD+, noncompetitive to L-threonine
NADH
-
competitive inhibition vs. NAD+, noncompetitive vs. L-threonine
NADH
-
competitive inhibition vs. NAD+, noncompetitive vs. L-threonine
Ni2+
-
3.2 mM, 20-50% inhibition
Ni2+
-
3.2 mM, 69% inhibition
Ni2+
-
1 mM, 40-50% inhibition
p-mercuribenzoate
-
-
p-mercuribenzoate
-
10fold excess leads to immidiate inactivation
p-mercuribenzoate
-
0.0013 mM, 75% inhibition, completely reversed within 20 min by addition of 0.02-0.2 mM 2-mercaptoethanol or dithiothreitol
pyruvate
competitive to L-threonine
pyruvate
-
20% inhibition at 10 mM
Zn2+
0.9 mM, 23% inhibiton
Zn2+
-
0.05 and 1.0 mM, 90% inhibition
additional information
no inhibition by Ni2+, Ca2+, Mg2+, Mn2+
-
additional information
-
no inhibition by Ni2+, Ca2+, Mg2+, Mn2+
-
additional information
poor inhibition by K[Fe(CN)6], no inhibition by ethylene diamine tetraacetic acid and ethylene glycol tetraacetic acid, and by trypsin inhibitor T-9378
-
additional information
-
poor inhibition by K[Fe(CN)6], no inhibition by ethylene diamine tetraacetic acid and ethylene glycol tetraacetic acid, and by trypsin inhibitor T-9378
-
additional information
-
L-ThrDH is unaffected by EDTA, Li2SO4, MgCl2, MnCl2, CaCl2, NiCl2, CoCl2, BaCl2, HgCl2, CdSO4, CuSO4, ZnCl2, or iodoacetic acid, each at 1 mM
-
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0.36
(R)-(-)-1-amino-2-propanol
25°C, pH 10, mutant enzyme G114A
-
0.2225
ethanol
at pH 8.8 and 37°C
0.00057 - 246
L-threonine
0.00802
n-butanol
at pH 8.8 and 37°C
additional information
additional information
-
0.061
L-serine
25°C, pH 10, wild-type enzyme
0.18
L-serine
25°C, pH 10, mutant enzyme G114A
1.6
L-serine
25°C, pH 10, mutant enzyme T178A
1.8
L-serine
25°C, pH 10, mutant enzyme I113A
0.00057
L-threonine
25°C, pH 10, mutant enzyme G114A
0.0026
L-threonine
25°C, pH 10, wild-type enzyme
0.0088
L-threonine
25°C, pH 10, mutant enzyme I113A
0.011
L-threonine
25°C, pH 10, mutant enzyme T178A
0.01129
L-threonine
at pH 8.8 and 37°C
0.0118
L-threonine
pH 7.5, 65°C, recombinant wild-type enzyme
0.013
L-threonine
-
pH 7.5, 65°C
0.043
L-threonine
25°C, pH 10, mutant enzyme D180A
1.1
L-threonine
-
metal-ion free enzyme
1.1
L-threonine
-
demetallized enzyme
1.5
L-threonine
-
pH 7.0, 70°C, recombinant enzyme
1.51
L-threonine
pH 7.5, 65°C, recombinant mutant E199A
1.6
L-threonine
-
at 50°C
2.5
L-threonine
pH 7.5, 65°C, recombinant mutant R204A
3.56
L-threonine
pH 9.0, 20°C
3.81
L-threonine
pH 9.0, 10°C
5.96
L-threonine
pH 9.0, 30°C
8.2
L-threonine
-
enzyme activated with 0.07 mM Cd2+
10.5
L-threonine
-
at pH 7.5
11.2
L-threonine
pH 9.0, 40°C
11.6
L-threonine
pH 10.0, 30°C, native enzyme
15.2
L-threonine
-
wild type enzyme, at pH 10.0 and 30°C
17.5
L-threonine
-
pH 10.0, 70°C
18
L-threonine
pH 9.0, 37°C
19.5
L-threonine
pH 9.0, 50°C
23.7
L-threonine
30°C, pH not specified in the publication, mutant enzyme T177A
25.3
L-threonine
30°C, pH not specified in the publication, wild-type enzyme
40.6
L-threonine
30°C, pH not specified in the publication, mutant enzyme Y136F
72.4
L-threonine
wild type enzyme, at pH 7.5 and 37°C
151.9
L-threonine
mutant enzyme M333E, at pH 7.5 and 37°C
211
L-threonine
-
enzyme activated with 0.25 mM Mn2+
221
L-threonine
-
enzyme saturated with 0.25 mM Mn2+
246
L-threonine
30°C, pH not specified in the publication, mutant enzyme S111A
0.0099
NAD+
pH 7.5, 65°C, recombinant wild-type enzyme
0.0099
NAD+
-
pH 7.5, 65°C, recombinant wild-type enzyme
0.014
NAD+
30°C, pH not specified in the publication, mutant enzyme S74A
0.0155
NAD+
30°C, pH not specified in the publication, mutant enzyme D179N
0.0196
NAD+
30°C, pH not specified in the publication, mutant enzyme S111A
0.0243
NAD+
30°C, pH not specified in the publication, mutant enzyme D179A
0.0257
NAD+
30°C, pH not specified in the publication, mutant enzyme T177A
0.0507
NAD+
30°C, pH not specified in the publication, wild-type enzyme
0.055
NAD+
-
pH 7.0, 70°C, recombinant enzyme
0.0615
NAD+
pH 7.5, 65°C, recombinant mutant E152A
0.097
NAD+
-
mutant enzyme T186N, at pH 10.0 and 30°C
0.1
NAD+
pH 10.0, 30°C, native enzyme
0.11
NAD+
-
metal-ion free enzyme
0.11
NAD+
-
demetallized enzyme
0.115
NAD+
-
mutant enzyme L80G, at pH 10.0 and 30°C
0.12
NAD+
-
wild type enzyme, at pH 10.0 and 30°C
0.152
NAD+
pH 7.5, 65°C, recombinant mutant E152T
0.156
NAD+
-
mutant enzyme G184A, at pH 10.0 and 30°C
0.163
NAD+
pH 7.5, 65°C, recombinant mutant E152C
0.18
NAD+
-
enzyme activated with 0.07 mM Cd2+
0.185
NAD+
-
pH 10.0, 70°C
0.216
NAD+
pH 7.5, 65°C, recombinant mutant E152Q
0.291
NAD+
pH 7.5, 65°C, recombinant mutant R204A
0.304
NAD+
pH 7.5, 65°C, recombinant mutant E199A
0.399
NAD+
pH 7.5, 65°C, recombinant mutant E152D
0.428
NAD+
30°C, pH not specified in the publication, mutant enzyme Y136F
0.6
NAD+
-
enzyme activated with 0.25 mM Mn2+
0.6
NAD+
-
enzyme saturated with 0.25 mM Mn2+
0.607
NAD+
pH 7.5, 65°C, recombinant mutant E152S
1.67
NAD+
wild type enzyme, at pH 7.5 and 37°C
2.06
NAD+
mutant enzyme R180K, at pH 7.5 and 37°C
additional information
additional information
-
kinetics
-
additional information
additional information
kinetic analysis of Glu152 mutants, overview
-
additional information
additional information
-
kinetic analysis of Glu152 mutants, overview
-
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-
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74
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brenda
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89
770-776
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Gallus gallus, Gallus gallus ROSS 308
brenda
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85
e01807-19
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brenda
Motoyama, T.; Nakano, S.; Yamamoto, Y.; Tokiwa, H.; Asano, Y.; Ito, S.
Product release mechanism associated with structural changes in monomeric L-threonine 3-dehydrogenase
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56
5758-5770
2017
uncultured archaeon (D6PBM7)
brenda
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SATB1 promotion of trophoblast stem cell renewal through regulation of threonine dehydrogenase
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1865
129757
2021
Rattus norvegicus (D3ZN15)
brenda