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EC Tree
IUBMB 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.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
threonine dehydrogenase, l-threonine dehydrogenase, l-threonine 3-dehydrogenase, l-thrdh, thrdh,
orf382 , thr dehydrogenase, threonine 3-dehydrogenase,
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L-threonine dehydrogenase
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threonine 3-dehydrogenase
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threonine dehydrogenase
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L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
ordered bi-bi mechanism, NAD+ binds prior to L-threonine
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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.
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DL-threo-3-hydroxynorvaline + NAD+
? + NADH
31% the rate of L-threonine
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?
L-threonine + 3-acetyl-pyridine adenine dinucleotide
L-2-amino-3-oxobutanoate + ?
60.6% the rate of NAD+
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?
L-threonine + 3-pyridinealdehyde adenine dinucleotide
L-2-amino-3-oxobutanoate + ?
7.2% the rate of NAD+
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?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
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?
L-threonine + nicotinamide guanine dinucleotide
L-2-amino-3-oxobutanoate + ?
5.1% the rate of NAD+
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?
L-threonine + thionicotinamide-NAD+
L-2-amino-3-oxobutanoate + ?
5.1% the rate of NAD+
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?
additional information
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additional information
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specific for L-form of threonine, no substrate: NADP, nicotinic acid adenine dinucleotide, alpha-NAD, nicotinamide hypoxanthine dinucleotide
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?
additional information
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specific for L-form of threonine, no substrate: NADP, nicotinic acid adenine dinucleotide, alpha-NAD, nicotinamide hypoxanthine dinucleotide
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?
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3-acetyl-pyridine adenine dinucleotide
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nicotinamide guanine dinucleotide
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adenosine-5'-diphosphoribose
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CuCl2
1 mM, 100% inhibition
HgCl2
10 mM, 100% inhibition
monoiodoacetate
10 mM, 100% inhibition
N-ethylmaleimide
10 mM, 48% inhibition
NADH
competitive to NAD+, noncompetitive to L-threonine
p-chloromercuribenzoic acid
10 mM, 44% inhibition
pyruvate
competitive to L-threonine
ZnCl2
1 mM, 72% inhibition
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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]
Neoplasms
THE EFFECT OF TUMOR GROWTH ON HEPATIC THREONINE DEHYDROGENASE.
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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
11.2
L-threonine
pH 9.0, 40°C
19.5
L-threonine
pH 9.0, 50°C
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0.37 - 1.42
adenosine-5'-diphosphoribose
0.37
adenosine-5'-diphosphoribose
substrate NAD+, pH 9.0, 30°C
1.42
adenosine-5'-diphosphoribose
substrate L-threonine, pH 9.0, 30°C
23.2
pyruvate
substrate L-threonine, pH 9.0, 30°C
50.7
pyruvate
substrate NAD+, pH 9.0, 30°C
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10.5
31% of maximum activity
8.5
74% of maximum activity
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10 - 30
60 min, more than 90% residual activity
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Swissprot
brenda
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Swissprot
brenda
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Q8KZM4_FLAFR
312
0
35412
TrEMBL
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35000
4 * 35000, SDS-PAGE
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homotetramer
4 * 35000, SDS-PAGE
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-20°C, 10 mM potassium phosphate, pH 7.0, 30% sucrose, 0.1 mM NAD+, 5 mM L-threonine, several months, no loss of activity
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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