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Information on EC 1.1.1.103 - L-threonine 3-dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P07913

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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:
Escherichia coli
UNIPROT: P07913
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The taxonomic range for the selected organisms is: Escherichia coli
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
citric acid + NAD+
?
show the reaction diagram
low activity
-
-
?
D-glucose + NAD+
?
show the reaction diagram
-
-
-
?
D-threonine + NAD+
(2R)-2-amino-3-oxobutanoate + NADH + H+
show the reaction diagram
lowest activity
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
show the reaction diagram
high activity
-
-
?
glycerol + NAD+
?
show the reaction diagram
-
-
-
?
isopropanol + NAD+
isopropylaldehyde + NADH + H+
show the reaction diagram
-
-
-
?
L-serine + NAD+
3-oxo-L-alanine + NADH + H+
show the reaction diagram
-
-
-
?
L-threonine + NAD+
(2S)-2-amino-3-oxobutanoate + NADH + H+
show the reaction diagram
high activity
-
-
?
lactic acid + NAD+
?
show the reaction diagram
low activity
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
show the reaction diagram
low activity
-
-
?
n-butanol + NAD+
butanal + NADH + H+
show the reaction diagram
highest activity
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
the enzyme exhibits an apparent preference for NAD+ over NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
the protein contains 0.424 mol of Fe per mol
Zn2+
the protein contains 0.914 mol of Zn2+ per mol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2225
ethanol
at pH 8.8 and 37°C
0.01129
L-threonine
at pH 8.8 and 37°C
0.00802
n-butanol
at pH 8.8 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
x * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team