Information on EC 1.1.1.103 - L-threonine 3-dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
1.1.1.103
-
RECOMMENDED NAME
GeneOntology No.
L-threonine 3-dehydrogenase
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
aminopropanol phosphate biosynthesis II
-
Glycine, serine and threonine metabolism
-
NIL
-
threonine degradation II
-
threonine degradation III (to methylglyoxal)
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L-ThrDH
Pyrococcus horikoshii OT-3
-
-
-
L-threonine dehydrogenase
-
-
-
-
L-threonine dehydrogenase
-
-
L-threonine dehydrogenase
-
-
L-threonine dehydrogenase
-
-
L-threonine dehydrogenase
O58389
-
L-threonine dehydrogenase
Pyrococcus horikoshii OT-3
-
-
-
L-threonine dehydrogenase
Q5JI69
-
L-threonine dehydrogenase
-
-
ThrDH
E5RQ20
-
threonine 3-dehydrogenase
-
-
-
-
threonine dehydrogenase
-
-
-
-
threonine dehydrogenase
-
-
threonine dehydrogenase
-
-
L-threonine dehydrogenase
-
-
additional information
O58389
the enzyme belongs to the medium-chain NAD(H)-dependent alcohol dehydrogenases
CAS REGISTRY NUMBER
COMMENTARY
9067-99-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
goat
-
-
Manually annotated by BRENDA team
Japanese quail, fed a standard or threonine-rich diet or fasted for three days
-
-
Manually annotated by BRENDA team
strain KUC-1
Q8KZM4
Swissprot
Manually annotated by BRENDA team
Cytophaga sp. KUC-1
strain KUC-1
Q8KZM4
Swissprot
Manually annotated by BRENDA team
strain MDS42, which lacks 14.3% of its chromosome
-
-
Manually annotated by BRENDA team
Escherichia coli MDS42
strain MDS42, which lacks 14.3% of its chromosome
-
-
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
orf PH0655, gene TDH
-
-
Manually annotated by BRENDA team
strain OT3
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
strain OT3
-
-
Manually annotated by BRENDA team
male Wistar albino, fed a standard diet or fasted for three days
-
-
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-, E5RQ20
14% activation at 10 mM
DTT
-, E5RQ20
25% activation at 10 mM
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
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.37
-
adenosine-5'-diphosphoribose
-, Q8KZM4
substrate NAD+, pH 9.0, 30C
1.42
-
adenosine-5'-diphosphoribose
-, Q8KZM4
substrate L-threonine, pH 9.0, 30C
23.2
-
pyruvate
-, Q8KZM4
substrate L-threonine, pH 9.0, 30C
50.7
-
pyruvate
-, Q8KZM4
substrate NAD+, pH 9.0, 30C
PDB
SCOP
CATH
ORGANISM
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
11
-, E5RQ20
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
4.5
9.5
-
purified recombinant enzyme, 20 min, 50C, no loss in activity
5.5
7.5
-
activity at pH 5.5 is 50% of that at pH 7.5
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
most stable in Tris-HCl, pH 8, purified preparations in phosphate buffers lose their activity overnight
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 10 mM potassium phosphate, pH 7.0, 30% sucrose, 0.1 mM NAD+, 5 mM L-threonine, several months, no loss of activity
-, Q8KZM4
4C, 50 mM Tris-HCl, pH 8.4, 1 mM 2-mercaptoethanol, 2 months, no loss of activity
-
-20C, 14 mM 2-mercaptoethanol, 20% glycerol, at least 1 month, little loss of activity
-
50 mM TrisHCl buffer, pH 8.0
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
synthesis
Escherichia coli MDS42
-
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
-