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Information on EC 1.1.1.103 - L-threonine 3-dehydrogenase and Organism(s) Mus musculus and UniProt Accession Q8K3F7

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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:
Mus musculus
UNIPROT: Q8K3F7
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The taxonomic range for the selected organisms is: Mus musculus
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, threonine 3-dehydrogenase, thr dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-threonine dehydrogenase
-
L-threonine dehydrogenase
threonine 3-dehydrogenase
-
-
-
-
threonine dehydrogenase
-
-
-
-
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
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
72.4 - 151.9
L-threonine
1.67 - 2.06
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
46.7 - 47.3
L-threonine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.7
L-threonine
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
predicted from gene sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Swissprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
most abundant
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
knockdown of the enzyme and posttranslational downregulation by microRNA-9 inhibits reprogramming efficiency
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TDH_MOUSE
373
0
41462
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41500
x * 41500, deduced from gene sequence, aminoterminal mitochondrial targeting sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 41500, deduced from gene sequence, aminoterminal mitochondrial targeting sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M333A
inactive
M333E
the mutation affects the substrate's affinity for the enzyme
R180K
the mutation has little effect on NAD+ binding affinity, whereas affects the substrate's affinity for the enzyme
S133A
inactive
T237A
inactive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-chelating column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team