BRENDA home
History
Information on EC 1.1.1.103 - L-threonine 3-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.103Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.1.103 L-threonine 3-dehydrogenaseIUBMB Comments
This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex . In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
CLOST_1621, L-ThrDH, L-threonine dehydrogenase, More, orf382, TDG, TDH, Thr dehydrogenase, ThrDH, threonine 3-dehydrogenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CLOST_1621
L-ThrDH
L-threonine dehydrogenase
TDH
ThrDH
threonine 3-dehydrogenase
-
-
-
-
threonine dehydrogenase
additional information
the enzyme belongs to the medium-chain NAD(H)-dependent alcohol dehydrogenases
L-threonine dehydrogenase
-
-
-
-
threonine dehydrogenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
it is suggested that the unstable L-2-amino-3-oxobutanoate spontaneousely decarboxylates to the stable aminoacetone, there is also some evidence that L-threonine is oxidatively decarboxylated by threonine dehydrogenase to produce aminoacetone
-
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
ordered bi-bi mechanism, NAD+ binds prior to L-threonine
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
His94 is an active site residue, substrate binding involved residues Gly66, Gly71, Gly77, and Val80
-
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
reaction mechanism, random bi bi kinetic mechanism
-
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
catalytic mechanism, the carboxyl group of Glu152 is important for expressing the catalytic activity, the proton relay system works as a catalytic mechanism of TDH
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
reaction mechanism involving catalytic residues T112, Y137, and K141, overview
-
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
ordered bi-bi mechanism, NAD+ binds prior to L-threonine
-
-
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
reaction mechanism, random bi bi kinetic mechanism
-
-
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-threonine:NAD+ oxidoreductase
This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [2]. In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9067-99-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
D-threonine + NAD+
(2R)-2-amino-3-oxobutanoate + NADH + H+
lowest activity
-
-
?
DL-threonine hydroxamate + NAD+
DL-2-amino-3-oxobutoxamate + NADH
-
-
-
?
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+
-
-
?
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
-
21% of the activity with L-threonine
-
-
?
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+
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+
-
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+
-
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 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
-
-
-
?
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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+
-
-
-
?
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+
-
-
-
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+
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
NAD+
binding site of the essential co-factor NAD+ is present in all subunits, it occupies the active site pocket and is bound predominantly by Van der Waal interactions and hydrogen bonds with the surrounding amino acid residues
NAD+
NADP+, thio-NAD+, or 3-acetylpyridine adenine dinucleotide cannot substitute for NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
Co2+
Cu2+
Mg2+
Mn2+
Zn2+
additional information
Cd2+
-
preincubation with 0.07 or 5 mM leads to 3fold increase of C38D mutant enzyme activity, 0.5 mM, 6.5fold increase of wild-type enzyme activity, substrate L-threonine
Cd2+
-
0.064 or 3.2 mM, 6fold increase of L-threonine dehydrogenase activity
Mn2+
-
preincubation with 1 mM, 3.5fold increase of L-threonine oxidation
Mn2+
-
0.064 or 3.2 mM, 4fold increase of L-threonine dehydrogenase activity, activation is dependent on the presence of a reduced thiol in all enzyme stock solutions and assay buffers, binding of 0.86 mol of Mn2+ per mol of enzyme subunit
Zn2+
-
5 mM, 60fold increase of C38D mutant enzyme activity, Zn2+ stimulated activity decreases to 10% when 1 mM Mn2+ is added, no increase in activity for wild-type enzyme
Zn2+
-
exchange of Zn2+ with Co2+ or Cd2+ does not change the specific activity of the enzyme
Zn2+
-
2 Zn2+ per enzyme subunit, binding involves residues G168, G175, G180, and G212, overview
Zn2+
1.22 mol of Zn2+ per mol of enzyme subunit, the catalytic zinc atom at the active center of TDH is coordinated by the highly conserved four residues Cys42, His67, Glu68 and Glu152 with low affinity
Zn2+
one molecule of TDH contains one zinc ion playing a structural role, the metal ion is ligated by foru Cys residues, coenzyme-binding domain shows a larger interdomain cleft compared to other ADHs, binding structure, overview
Zn2+
-
four zinc-binding cysteine residues, 0.1 mM reactivates EDTA-100% inhibited enzyme by 75%, 0.05 mM reactivates by 100%
additional information
no effect at 1 mM by AgNO3, MgCl2, and 10 mM EDTA and ethylene glycol tetraacetic acid
additional information
-
no effect at 1 mM by AgNO3, MgCl2, and 10 mM EDTA and ethylene glycol tetraacetic acid
additional information
the active site catalytic zinc ion is absent from the TDH structure
additional information
-
the active site catalytic zinc ion is absent from the TDH structure
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
dipicolinic acid
-
40 mM, 99% inhibition after 1 h, complete loss of enzyme-bound Zn2+
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
thionitrobenzoate
-
40fold molar excess, gradual 99% loss of enzyme activity
adenosine-5'-diphosphoribose
-
competive inhibition vs. NAD+, noncompetitive inhibition vs. L-threonine
EDTA
-
50 mM, 99% inhibition after 1 h, complete loss of enzyme-bound Zn2+
EDTA
-
retains 65% of its original activity after dialysis at 48ĆĀ°C against a buffer containing 1 mM EDTA. Activity is lost when TDH is heated at 60ĆĀ°C for 40 min and in boiling water for 5 min in the presence of 1 mM EDTA
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
p-mercuribenzoate
-
0.0013 mM, 75% inhibition, completely reversed within 20 min by addition of 0.02-0.2 mM 2-mercaptoethanol or dithiothreitol
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acalculous Cholecystitis
[Changes in the L-serine and L-threonine dehydrogenase activities in the blood serum of those who worked in the cleanup of the aftermath of the accident at the Chernobyl Atomic Electric Power Station who became ill with chronic acalculous cholecystitis]
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0118
L-threonine
pH 7.5, 65ĆĀ°C, recombinant wild-type enzyme
0.0099
NAD+
pH 7.5, 65ĆĀ°C, recombinant wild-type enzyme
additional information
additional information
kinetic analysis of Glu152 mutants, overview
-
additional information
additional information
-
kinetic analysis of Glu152 mutants, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.42
adenosine-5'-diphosphoribose
substrate L-threonine, pH 9.0, 30ĆĀ°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.032
-
enzyme activity in mitochondrial extracts prepared from fresh mitochondria
0.062
-
enzyme activity in mitochondrial extracts after freezing the mitochondria for 2 weeks at -20ĆĀ°C
0.6
-
C38D mutant, incubated with 0.07 or 5 mM Cd2+ 15 min before assay
10.2
-
C38D mutant, incubated with 5 mM Zn2+ and 0.07 mM Cd2+ 15 min before assay
2
-
C38D mutant, incubated with 5 mM Zn2+ and 1 mM Mn2+ 15 min before assay
additional information
additional information
-
specific activity in animals fed a standard diet is 11times higher than in the liver of rats fed a standard diet. Enzyme activities in the livers of fasting and threonine-rich diet groups are three and two times higher than in the group fed with standard diet
additional information
-
specific activity in Japanese quail fed a standard diet is 11times higher than in the liver of rats fed a standard diet. Enzyme activities in the livers of fasting groups are the same level as in the group fed with standard diet
additional information
-
threonine sequestration in the portal drained viscera and liver, threonine flux, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
10.3
7.5
7.8
9
-
crude enzyme extracts from mitochondria frozen for 14 days and dialyzed
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 12
activity range, pH-dependent activity varies in different buffer systems, profile overview
9.2 - 12
-
22% of maximal activity at pH 9.2, 50% at pH 9.5, and 52% at pH 12.0
additional information
additional information
pH dependencies of wild-type enzyme and E152D mutant, overview
additional information
-
pH dependencies of wild-type enzyme and E152D mutant, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
65
70
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Japanese quail, fed a standard or threonine-rich diet or fasted for three days
-
-
brenda
-
-
-
brenda
male Wistar albino, fed a standard diet or fasted for three days
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
embryonic stem cells are critically dependent on the amino acid threonine, and threonine catabolism via the TDH enzyme is important to the growth and metabolic state of mouse embryonic stem cells
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
knockdown of the enzyme and posttranslational downregulation by microRNA-9 inhibits reprogramming efficiency
physiological function
additional information
evolution
the enzyme belongs to the extended short-chain alcohol dehydrogenase superfamily
evolution
-
the enzyme belongs to the extended short-chain alcohol dehydrogenase superfamily
-
physiological function
-
embryonic stem cells are critically dependent on the amino acid threonine, and threonine catabolism via the TDH enzyme is important to the growth and metabolic state of mouse embryonic stem cells
physiological function
-
over-expression of a feedback-resistant threonine operon thrA*BC, with deletion of the genes that encode threonine dehydrogenase tdh and threonine transporters tdcC and sstT, and introduction of a mutant threonine exporter rhtA23 in Escherichia coliMDS42. The resulting strain shows about 83% increase in L-threonine production when cells are grown by flask fermentation, compared to a wild-type Escherichia coli strain MG1655 engineered with the same threonine-specific modifications described above
physiological function
-
the enzyme plays an important role in the regulation of somatic cell reprogramming
physiological function
-
over-expression of a feedback-resistant threonine operon thrA*BC, with deletion of the genes that encode threonine dehydrogenase tdh and threonine transporters tdcC and sstT, and introduction of a mutant threonine exporter rhtA23 in Escherichia coliMDS42. The resulting strain shows about 83% increase in L-threonine production when cells are grown by flask fermentation, compared to a wild-type Escherichia coli strain MG1655 engineered with the same threonine-specific modifications described above
-
additional information
-
active site structure and subunit interaction, overview
additional information
the enzyme possesses a glycine-rich NAD+-binding domain at the N terminus and conserved catalytic triad of YxxxK residues
additional information
-
the enzyme possesses a glycine-rich NAD+-binding domain at the N terminus and conserved catalytic triad of YxxxK residues
additional information
-
the enzyme possesses a glycine-rich NAD+-binding domain at the N terminus and conserved catalytic triad of YxxxK residues
-
Show AA Sequence and Transmembrane Helices (11932 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
34628
2 x 37200, native enzyme, SDS-PAGE, x * 34628, sequence calculation
35000
36000
37742
-
2 * 36000-38000, recombinant enzyme, SDS-PAGE, 2 * 37742, sequence calculation
37823
-
4 * 40000, recombinant enzyme, SDS-PAGE, 4 * 37823, sequence calculation
38000
x * 38000, recombinant wild-type and mutant enzymes, SDS-PAGE
38016
40000
41200
-
4 * 41200, recombinant enzyme, SDS-PAGE, 4 * 41815, sequence calculation
41500
41815
-
4 * 41200, recombinant enzyme, SDS-PAGE, 4 * 41815, sequence calculation
36000
x * 41500, pro-protein, x * 36000, mature enzyme, deduced from gene sequence, aminoterminal mitochondrial targeting sequence
38016
4 * 38016, electrospray mass spectrometry and gel filtration
38016
-
4 * 38016, electrospray mass spectrometry and gel filtration
40000
-
4 * 40000, recombinant enzyme, SDS-PAGE, 4 * 37823, sequence calculation
41500
x * 41500, deduced from gene sequence, aminoterminal mitochondrial targeting sequence
41500
x * 41500, pro-protein, x * 36000, mature enzyme, deduced from gene sequence, aminoterminal mitochondrial targeting sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer
monomer
tetramer
additional information
?
x * 41500, deduced from gene sequence, aminoterminal mitochondrial targeting sequence
?
x * 41500, pro-protein, x * 36000, mature enzyme, deduced from gene sequence, aminoterminal mitochondrial targeting sequence
dimer
2 x 37200, native enzyme, SDS-PAGE, x * 34628, sequence calculation
dimer
-
2 x 37200, native enzyme, SDS-PAGE, x * 34628, sequence calculation
-
dimer
-
2 * 36000-38000, recombinant enzyme, SDS-PAGE, 2 * 37742, sequence calculation
homodimer
2 * 35000, SDS-PAGE, acitve in monomeric and in dimeric enzyme form
homodimer
-
2 * 35000, SDS-PAGE, acitve in monomeric and in dimeric enzyme form
-
homotetramer
4 * 38016, electrospray mass spectrometry and gel filtration
homotetramer
-
4 * 38016, electrospray mass spectrometry and gel filtration
tetramer
-
4 * 40000, recombinant enzyme, SDS-PAGE, 4 * 37823, sequence calculation
tetramer
-
4 * 41200, recombinant enzyme, SDS-PAGE, 4 * 41815, sequence calculation
tetramer
-
4 * 41200, recombinant enzyme, SDS-PAGE, 4 * 41815, sequence calculation
-
additional information
crystal structure analysis, each subunit is composed of two domains: an NAD(H)-binding domain and a catalytic domain. The NAD(H)-binding domain contains the alpha/beta Rossmann fold motif, characteristic of the NAD(H)-binding protein
additional information
-
crystal structure analysis, each subunit is composed of two domains: an NAD(H)-binding domain and a catalytic domain. The NAD(H)-binding domain contains the alpha/beta Rossmann fold motif, characteristic of the NAD(H)-binding protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
pro-protein is cleaved to produce a 36000 Da mature enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M CaCl2
-
apo form, in complex with NAD+ and glycerol, or with only NAD+, sitting drop vapor diffusion method, using 0.1 M HEPES (pH 7.0), 10% (w/v) PEG 4000, 10% (v/v) 2-propanol, or 0.2 M NaCl, 0.1 M HEPES (pH 7.5), 25% (w/v) PEG3350
purified recombinant enzyme, hanging drop vapour diffusion method, 4ĆĀ°C, 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 0.0015 ml of protein and reservoir solution are mixed, the reservoir solution contains 0.2 M NaCl, 0.1 M HEPES, pH 7.5, and 40% v/v PEG 400, 5 days, X-ray diffraction structure determination and preliminary analysis at 2.2 A resolution
-
selenomethionine-substituted enzyme, 10 mg/ml protein in 50 mM Tris-HCl buffer, pH 7.5, hanging-drop vapor-diffusion method at 4ĆĀ°C, mixing of 0.0015 ml of each, protein and reservoir solution, the latter containing 0.2 M sodium chloride, 0.1 M HEPES buffer, pH 7.5, and 40% v/v PEG 400, five days, X-ray diffraction structure determination and analysis, single wavelength anomalous diffraction method
at room temperature using hanging-drop vapour diffusion method, at 2.4 A resolution. The enzyme is a homotetramer, each monomer consisting of 350 amino acids that form two domains, a catalytic domain and a NAD+-binding domain, which contains an alpha/beta Rossmann fold motif. An extended twelve-stranded beta-sheet is formed by the association of pairs of monomers in the tetramer
by hanging-drop vapour-diffusion method, to 2.6 A resolution. Crystals grow in the tetragonal space group P43212, with unit-cell parameters a=b=124.5, c=271.1 A. There are four molecules in the asymmetric unit of the crystal
purified wild-type enzyme or enzyme mutant Y137F in complex with NAD+ and L-3-hydroxynorvaline or pyruvate or L-threonine, sitting drop vapor diffusion method, mixing of 0.001 ml of 40 mg/ml wild-type or 25 mg/ml mutant enzyme, and 1 mM NAD+ mixed with 0.001 ml of 100 mM cacodylate buffer, pH 6.4, 50% v/v 2-methyl-2,4-pentandiol, and 5% w/v PEG 8000, 20ĆĀ°C, crystals of ligand-bound wild-type or mutant enzymes by soaking the crystals in reservoir solution containing 0.3 M pyruvate for 2 h, or 0.1ML-threonine for 8 h or 0.1MDL-3-hydroxynorvaline for 7 h, respectively, X-ray diffraction structure determination and analysis at 1.77-2.07 A resolution, molecular replacement
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G184A
-
the catalytic efficiency of the mutant is 330fold lower than that of the wild type enzyme
L80G
-
the catalytic efficiency of the mutant is 3300fold lower than that of the wild type enzyme
T186N
-
the catalytic efficiency of the mutant is 330fold lower than that of the wild type enzyme
C38S
R180K
the mutation has little effect on NAD+ binding affinity, whereas affects the substrate's affinity for the enzyme
E152A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152C
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152D
site-directed mutagenesis, the E152D mutant shows 3-fold higher turnover rate and reduced affinities toward L-threonine and NAD+ compared to wild-type TDH, Glu152 to Asp substitution causes the enhancement of deprotonation of His47 or ionization of zinc-bound water and threonine in the enzyme-NAD+ complex
E152Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152T
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E199A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R204A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
additional information
C38S
-
site-directed mutagenesis, catalytically inactive mutant, C38 is located in an activating divalent metal-ion binding site
C38S
-
1 cysteine residue per subunit is essential for catalytic activity and Mn2+ binding
additional information
-
all individuals examined contain at least two mutations that on translation would generate truncated proteins that would be non-functional since they have lost the splicing acceptor site preceding exon 6 and codon Arg214 is mutated to a stop codon. Therefore the gene is an expressed pseudogene
additional information
-
ste11 gene knocked out with a double crossover via homologous recombination. Monosaccharide composition of exopolysaccharide produced by the mutant strain is altered from that of ebosin. Bioactivity of the mutant is lower than ebosin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11
the purified enzyme is very stable from pH 6.0 to pH 11.0 in the glycine-KOH system, the enzyme is unstable in sodium acetate buffer, pH 4.0-5.0, and Na2CO3-NaHCO3 buffer, pH 10.0-11.0
721272
4.5 - 9.5
-
purified recombinant enzyme, 20 min, 50ĆĀ°C, no loss in activity
722747
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
30 min, pH 7.0, over 90% remaining activity, purified recombinant enzyme
25 - 35
-
85% inactivation after 2 min at 35ĆĀ°C, 10% inactivation at 35ĆĀ°C in the presence of 80 mM KCl
25 - 45
-
enzyme shows 50% activity at 25ĆĀ°C compared with that at 35ĆĀ°C
80
-
60 min, pH 7.0, over 90% remaining activity, purified recombinant enzyme
85
-
the enzyme shows a half life of 2 h at 85ĆĀ°C and 24 min in boiling water
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
most stable in Tris-HCl, pH 8, purified preparations in phosphate buffers lose their activity overnight
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20ĆĀ°C, 10 mM potassium phosphate, pH 7.0, 30% sucrose, 0.1 mM NAD+, 5 mM L-threonine, several months, no loss of activity
-20ĆĀ°C, 14 mM 2-mercaptoethanol, 20% glycerol, at least 1 month, little loss of activity
-
4ĆĀ°C, 50 mM Tris-HCl, pH 8.4, 1 mM 2-mercaptoethanol, 2 months, no loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by heat treatment (about 80% pure recombinant TDH protein) and gel filtration
-
by sonication, centrifugation, heating of the soluble fraction, anion-exchange and hydrophobic interaction chromatography
by sonication, heating of the cell lysate, anion exchange and hydrophobic interaction chromatography
chromatography on Q-Sepharose and Reactive Green 19-agarose
DEAE Sepharose FF, Affi-Gel blue, Sephacryl S-200, Matrix Gel red A, Matrix gel Green A
-
DEAE-cellulose, ammonium sulfate, DEAE-cellulose, Blue dextran-Sepharose, Sephadex G-200, amylamine sepharose, Sephadex G-200
-
DEAE-cellulose, hydrophobic interaction chromatography, Affi-Gel Blue, Matrex Red A
-
MnCl2, ammonium sulfate, calcium phosphate gel, protamine sulfate, DEAE-cellulose, 7fold purification
-
recombinant enzyme 48fold from Escherichia coli to homogeneity by heat treatment and anion exchange chromatography
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 85ĆĀ°C for 30 min, centrifugation, ion exchange chromatography, and gel filtration
-
recombinant His-tagged enzyme 4.2fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, native enzyme 75.4fold by anion exchange and hydrophobic interaction chromatography, dialysis, hydroxyapatite chromatography, followed by gel filtration
recombinant His-tagged enzyme from Escherichia coli strain TOP10 by nickel affinity chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by heat treatment at 85ĆĀ°C for 30 min, anion exchange and hydrophobic interaction chromatography
treatment of cell extract at 60ĆĀ°C, DEAE-Sephadex, Mn2+ activation, Blue 2-Sepharose CL-6B, C38D mutant was purified without Mn2+ activation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid seuence determination and analysis, sequence comparisons, phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strains JM109 and BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
into pET-30a digested with KpnIĆ¢ĀĀEcoRI to construct pET-ste11 and expressed in Escherichia coli BL21
-
ligated into the pTZ57R/T cloning vector. The recombinant pTZ-tdh plasmid digested with NcoI and EcoRI and the TDH gene ligated with pET-8c, giving the recombinant pET-tdh plasmid, used to transform Escherichia coli DH5alpha competent cells. Recombinant and purified pET-tdh plasmid expressed in Escherichia coli BL21 (DE3)
orf PH0655, amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain TOP10
-
orf PH0655, gene TDH, overexpression in Escherichia coli strain BL21(DE3)
-
orf PH0655, NA and amino acid sequence determination, analysis, and comparison, expression of selenomethionine-labeled wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
orf PH0655, overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
plasmid pTZ-tdh transformed in Escherichia coli DH5alpha competent cells. NcoI-EcoRI restriction fragment inserted into the pET-8c expression vector at the corresponding sites. The resulting plasmid pET-tdh expressed in Escherichia coli strain BL21(DE3)CodonPlus-RIL
-
recombinant pET-tdh plasmid expressed in Escherichia coli BL21 (DE3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme activity is significantly increased with a diet containing soybean meal
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
over-expression of a feedback-resistant threonine operon thrA*BC, with deletion of the genes that encode threonine dehydrogenase tdh and threonine transporters tdcC and sstT, and introduction of a mutant threonine exporter rhtA23 in Escherichia coliMDS42. The resulting strain shows about 83% increase in L-threonine production when cells are grown by flask fermentation, compared to a wild-type Escherichia coli strain MG1655 engineered with the same threonine-specific modifications described above
synthesis
-
over-expression of a feedback-resistant threonine operon thrA*BC, with deletion of the genes that encode threonine dehydrogenase tdh and threonine transporters tdcC and sstT, and introduction of a mutant threonine exporter rhtA23 in Escherichia coliMDS42. The resulting strain shows about 83% increase in L-threonine production when cells are grown by flask fermentation, compared to a wild-type Escherichia coli strain MG1655 engineered with the same threonine-specific modifications described above
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yuan, J.H.; austic, R.E.
Characterization of hepatic L-threonine dehydrogenase of chicken
Comp. Biochem. Physiol. B
130
65-73
2001
Gallus gallus
brenda
Johnson, A.R.; Chen, Y.W.; Dekker, E.E.
Investigation of a catalytic zinc binding site in Escherichia coli L-threonine dehydrogenase by site-directed mutagenesis of cysteine-38
Arch. Biochem. Biophys.
358
211-221
1998
Escherichia coli K-12
brenda
Marcus, J.P.; Dekker, E.E.
Identification of a second active site residue in Escherichia coli L-threonine dehydrogenase: methylation of histidin-90 with methyl p-nitrobenzenesulfonate
Arch. Biochem. Biophys.
316
413-420
1995
Escherichia coli K-12
brenda
Chen, Y.W.; Dekker, E.E.; Somerville, R.L.
Functional analysis of E. coli threonine dehydrogenase by means of mutant isolation and characterization
Biochim. Biophys. Acta
1253
208-214
1995
Escherichia coli K-12
brenda
Kao, Y.C.; Davis, L.
Purification and structural characterization of porcine L-threonine dehydrogenase
Protein Expr. Purif.
5
423-431
1994
Sus scrofa
brenda
Marcus, J.P.; Dekker, E.E.
Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme A lyase and threonine dehydrogenase
J. Bacteriol.
175
6505-6511
1993
Escherichia coli K-12
brenda
Pagani, R.; Leoncini, R.; Righi, S.; Guerranti, R.; Lazzerretti, L.; Marinello, E.
Mitochondrial L-threonine dehydrogenase
Biochem. Soc. Trans.
20
379
1992
Rattus norvegicus
-
brenda
Pagani, R.; Guerranti, R.; Right, S.; Leoncini, R.; Vannoni, D.; Marinello, E.
Rat liver L-threonine dehydrogenase
Biochem. Soc. Trans.
20
24
1991
Bos taurus, Rattus norvegicus
-
brenda
Epperly, B.R.; Dekker, E.E.
L-Threonine dehydrogenase from Escherichia coli
J. Biol. Chem.
266
6086-6092
1991
Escherichia coli K-12
brenda
Craig, P.A.; Dekker, E.E.
The sulfhydryl content of L-threonine dehydrogenase from Escherichia coli K-12: relation to catalytic activity and Mn2+ activation
Biochim. Biophys. Acta
1037
30-38
1990
Escherichia coli K-12
brenda
Aronson, B.D.; Somerville, R.L.; Epperly, B.R.; Dekker, E.E.
The primary structure of Escherichia coli L-threonine dehydrogenase
J. Biol. Chem.
264
5226-5232
1989
Escherichia coli K-12
brenda
Craig, P.A.; Dekker, E.E.
Cd2+ activation of L-threonine dehydrogenase from Escherichia coli K-12
Biochim. Biophys. Acta
957
222-229
1988
Escherichia coli K-12
brenda
Tressel, T.; Thompson, R.; Zieske, L.R.; Menendez, M.I.T.S.; Davis, L.
Interaction between L-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production
J. Biol. Chem.
261
16428-16437
1986
Sus scrofa
brenda
Craig, P.A.; Dekker, E.E.
L-Threonine dehydrogenase from Escherichia coli K-12: thiol-dependent activation by Mn2+
Biochemistry
25
1870-1876
1986
Escherichia coli K-12
brenda
Ray, M.; Ray, S.
L-Threonine dehydrogenase from goat liver
J. Biol. Chem.
260
5913-5918
1985
Capra hircus
brenda
Boylan, S.A.; Dekker, E.E.
L-threonine dehydrogenase
J. Biol. Chem.
256
1809-1815
1981
Escherichia coli K-12
brenda
Aoyama, Y.; Motokawa, Y.
L-Threonine dehydrogenase of chicken liver
J. Biol. Chem.
256
12367-12373
1981
Gallus gallus
brenda
Boylan, S.A.; Dekker, E.E.
L-Threonine dehydrogenase of Escherichia coli K-12
Biochem. Biophys. Res. Commun.
85
190-197
1978
Escherichia coli K-12
brenda
McGilvray, D.; Morris, J.G.
L-Threonine dehydrogenase (Arthrobacter)
Methods Enzymol.
17B
580-584
1971
Arthrobacter sp.
-
brenda
Green, M.L.; Elliott, W.H.
The enzymatic formation of aminoacetone from threonine and its further metabolism
biochem. J.
92
537-548
1964
Gallus gallus, Oryctolagus cuniculus, Staphylococcus aureus, Rattus norvegicus, Sus scrofa
brenda
Hartshorne, D.; Greenberg, D.M.
Studies on liver threonine dehydrogenase
Arch. Biochem. Biophys.
105
173-178
1964
Lithobates catesbeianus
brenda
Akagi, S.; Sato, K.; Ohmori, S.
Threonine metabolism in Japanese quail liver
Amino Acids
26
235-242
2004
Coturnix japonica, Rattus norvegicus
brenda
Edgar, A.J.
Molecular cloning and tissue distribution of mammalian L-threonine 3-dehydrogenases
BMC Biochem.
3
19
2002
Mus musculus (Q8K3F7), Mus musculus, Sus scrofa (Q8MIR0), Sus scrofa
brenda
Edgar, A.J.
The human L-threonine 3-dehydrogenase gene is an expressed pseudogene
BMC Genet.
3
18
2002
Homo sapiens
brenda
Kazuoka, T.; Takigawa, S.; Arakawa, N.; Hizukuri, Y.; Muraoka, I.; Oikawa, T.; Soda, K.
Novel psychrophilic and thermolabile L-threonine dehydrogenase from psychrophilic Cytophaga sp. strain KUC-1
J. Bacteriol.
185
4483-4489
2003
Cytophaga sp. (Q8KZM4), Cytophaga sp., Cytophaga sp. KUC-1 (Q8KZM4)
brenda
Higashi, N.; Matsuura, T.; Nakagawa, A.; Ishikawa, K.
Crystallization and preliminary X-ray analysis of hyperthermophilic L-threonine dehydrogenase from the archaeon Pyrococcus horikoshii
Acta crystallogr. Sect. F
61
432-434
2005
Pyrococcus horikoshii
brenda
Le Floch, N.; Seve, B.
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
Br. J. Nutr.
93
447-456
2005
Sus scrofa
brenda
Shimizu, Y.; Sakuraba, H.; Kawakami, R.; Goda, S.; Kawarabayasi, Y.; Ohshima, T.
L-Threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3: gene cloning and enzymatic characterization
Extremophiles
9
317-324
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Machielsen, R.; van der Oost, J.
Production and characterization of a thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
FEBS J.
273
2722-2729
2006
Pyrococcus furiosus
brenda
Higashi, N.; Fukada, H.; Ishikawa, K.
Kinetic study of thermostable L-threonine dehydrogenase from an archaeon Pyrococcus horikoshii
J. Biosci. Bioeng.
99
175-180
2005
Pyrococcus horikoshii
brenda
Higashi, N.; Tanimoto, K.; Nishioka, M.; Ishikawa, K.; Taya, M.
Investigating a catalytic mechanism of hyperthermophilic L-threonine dehydrogenase from Pyrococcus horikoshii
J. Biochem.
144
77-85
2008
Pyrococcus horikoshii (O58389), Pyrococcus horikoshii
brenda
Ishikawa, K.; Higashi, N.; Nakamura, T.; Matsuura, T.; Nakagawa, A.
The first crystal structure of L-threonine dehydrogenase
J. Mol. Biol.
366
857-867
2007
Pyrococcus horikoshii (O58389), Pyrococcus horikoshii
brenda
Bowyer, A.; Mikolajek, H.; Wright, J.N.; Coker, A.; Erskine, P.T.; Cooper, J.B.; Bashir, Q.; Rashid, N.; Jamil, F.; Akhtar, M.
Crystallization and preliminary X-ray diffraction analysis of L-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis
Acta Crystallogr. Sect. F
64
828-830
2008
Thermococcus kodakarensis (Q5JI69), Thermococcus kodakarensis
brenda
Bao, Y.; Xie, H.; Shan, J.; Jiang, R.; Zhang, Y.; Guo, L.; Zhang, R.; Li, Y.
Biochemical characteristics and function of a threonine dehydrogenase encoded by ste11 in Ebosin biosynthesis of Streptomyces sp. 139
J. Appl. Microbiol.
106
1140-1146
2009
Streptomyces sp. 139
brenda
Bashir, Q.; Rashid, N.; Jamil, F.; Imanaka, T.; Akhtar, M.
Highly thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis
J. Biochem.
146
95-102
2009
Thermococcus kodakarensis KOD1
brenda
Bowyer, A.; Mikolajek, H.; Stuart, J.W.; Wood, S.P.; Jamil, F.; Rashid, N.; Akhtar, M.; Cooper, J.B.
Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis
J. Struct. Biol.
168
294-304
2009
Thermococcus kodakarensis (Q5JI69), Thermococcus kodakarensis
brenda
Lee, J.H.; Sung, B.H.; Kim, M.S.; Blattner, F.R.; Yoon, B.H.; Kim, J.H.; Kim, S.C.
Metabolic engineering of a reduced-genome strain of Escherichia coli for L-threonine production
Microb. Cell Fact.
8
02
2009
Escherichia coli, Escherichia coli MDS42
brenda
Wang, J.; Alexander, P.; Wu, L.; Hammer, R.; Cleaver, O.; McKnight, S.L.
Dependence of mouse embryonic stem cells on threonine catabolism
Science
325
435-439
2009
Mus musculus
brenda
Ueatrongchit, T.; Asano, Y.
Highly selective L-threonine 3-dehydrogenase from Cupriavidus necator and its use in determination of L-threonine
Anal. Biochem.
410
44-56
2011
Cupriavidus necator (E5RQ20), Cupriavidus necator, Cupriavidus necator NBRC 102504 (E5RQ20), Cupriavidus necator NBRC 102504
brenda
Yoneda, K.; Sakuraba, H.; Araki, T.; Ohshima, T.
Crystal structure of binary and ternary complexes of archaeal UDP-galactose 4-epimerase-like L-threonine dehydrogenase from Thermoplasma volcanium
J. Biol. Chem.
287
12966-12974
2012
Thermoplasma volcanium
brenda
Han, C.; Gu, H.; Wang, J.; Lu, W.; Mei, Y.; Wu, M.
Regulation of L-threonine dehydrogenase in somatic cell reprogramming
Stem Cells
31
953-965
2013
Mus musculus
brenda
Wagner, M.; Andreesen, J.R.
Purification and characterization of threonine dehydrogenase from Clostridium sticklandi
Arch. Microbiol.
163
286-290
1995
Acetoanaerobium sticklandii (E3PS87), Acetoanaerobium sticklandii, Acetoanaerobium sticklandii DSM 519 (E3PS87)
brenda
Lee, C.; Cho, I.; Lee, Y.; Son, Y.; Kwak, I.; Ahn, Y.; Kim, S.; An, W.
Effects of dietary levels of glycine, threonine and protein on threonine efficiency and threonine dehydrogenase activity in hepatic mitochondria of chicks
Asian-australas. J. Anim. Sci.
27
69-76
2014
Gallus gallus
brenda
Nakano, S.; Okazaki, S.; Tokiwa, H.; Asano, Y.
Binding of NAD+ and L-threonine induces stepwise structural and flexibility changes in Cupriavidus necator L-threonine dehydrogenase
J. Biol. Chem.
289
10445-10454
2014
Cupriavidus necator
brenda
Ma, F.; Wang, T.; Ma, X.; Wang, P.
Identification and characterization of protein encoded by orf382 as L-threonine dehydrogenase
J. Microbiol. Biotechnol.
24
748-755
2014
Escherichia coli (P07913), Escherichia coli
brenda
He, C.; Huang, X.; Liu, Y.; Li, F.; Yang, Y.; Tao, H.; Han, C.; Zhao, C.; Xiao, Y.; Shi, Y.
Structural insights on mouse L-threonine dehydrogenase: A regulatory role of Arg180 in catalysis
J. Struct. Biol.
192
510-518
2015
Mus musculus (Q8K3F7), Mus musculus
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.1.1.103)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
About BRENDA
Help
Download
Contribution
member of
curated at
curated at
Server: brenda5 Ver: 69ad221-main (2022-06-24 14:26:09 +0200)