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Information on EC 1.1.1.103 - L-threonine 3-dehydrogenase

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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.
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This record set is specific for:
UNIPROT: Q8KZM4
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-threonine dehydrogenase
-
-
-
-
threonine 3-dehydrogenase
-
-
-
-
threonine dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+
show the reaction diagram
ordered bi-bi mechanism, NAD+ binds prior to L-threonine
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9067-99-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DL-threo-3-hydroxynorvaline + NAD+
? + NADH
show the reaction diagram
31% the rate of L-threonine
-
-
?
L-threonine + 3-acetyl-pyridine adenine dinucleotide
L-2-amino-3-oxobutanoate + ?
show the reaction diagram
60.6% the rate of NAD+
-
-
?
L-threonine + 3-pyridinealdehyde adenine dinucleotide
L-2-amino-3-oxobutanoate + ?
show the reaction diagram
7.2% the rate of NAD+
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
L-threonine + nicotinamide guanine dinucleotide
L-2-amino-3-oxobutanoate + ?
show the reaction diagram
5.1% the rate of NAD+
-
-
?
L-threonine + thionicotinamide-NAD+
L-2-amino-3-oxobutanoate + ?
show the reaction diagram
5.1% the rate of NAD+
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetyl-pyridine adenine dinucleotide
-
nicotinamide guanine dinucleotide
-
thionicotinamide-NAD+
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine-5'-diphosphoribose
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.56 - 19.5
L-threonine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37 - 1.42
adenosine-5'-diphosphoribose
23.2 - 50.7
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
156
pH 9.0, 20°C
284
pH 9.0, 30°C
611
pH 9.0, 50°C
722
pH 9.0, 40°C
91.4
pH 9.0, 10°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.5
31% of maximum activity
8.5
74% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 30
60 min, more than 90% residual activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Swissprot
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8KZM4_FLAFR
312
0
35412
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
139000
gel filtration
35000
4 * 35000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 35000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
half-life 160 min
45
half-life 14 min
50
rapid inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team