Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ueatrongchit, T.; Asano, Y.
    Highly selective L-threonine 3-dehydrogenase from Cupriavidus necator and its use in determination of L-threonine (2011), Anal. Biochem., 410, 44-56.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.103 2-mercaptoethanol 14% activation at 10 mM Cupriavidus necator
1.1.1.103 DTT 25% activation at 10 mM Cupriavidus necator

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.103 DNA and amino acid seuence determination and analysis, sequence comparisons, phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strains JM109 and BL21(DE3) Cupriavidus necator

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.103 4-chloromercuribenzonic acid 94% inhibition at 10 mM Cupriavidus necator
1.1.1.103 calcium pantothenate slight inhibition Cupriavidus necator
1.1.1.103 FeCl2 32% inhibition at 1 mM after 60 min Cupriavidus necator
1.1.1.103 FeCl3 73% inhibition at 1 mM after 60 min Cupriavidus necator
1.1.1.103 HgCl2 77% inhibition at 1 mM after 60 min Cupriavidus necator
1.1.1.103 iodoacetamide 99% inhibition at 10 mM Cupriavidus necator
1.1.1.103 iodoacetic acid 52% inhibition at 10 mM Cupriavidus necator
1.1.1.103 K3[Fe(CN)6] 25% inhibition at 10 mM Cupriavidus necator
1.1.1.103 additional information poor inhibition by K[Fe(CN)6], no inhibition by ethylene diamine tetraacetic acid and ethylene glycol tetraacetic acid, and by trypsin inhibitor T-9378 Cupriavidus necator
1.1.1.103 N-ethylmaleimide complete inhibition Cupriavidus necator
1.1.1.103 NaN3 88% inhibition at 10 mM Cupriavidus necator
1.1.1.103 phenazinemethosulfate complete inhibition Cupriavidus necator
1.1.1.103 phenylmethanesulfonyl fluoride 63% inhibition at 10 mM Cupriavidus necator
1.1.1.103 SnCl2 16% inhibition at 1 mM after 60 min Cupriavidus necator

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.103 0.1
-
 NAD+ pH 10.0, 30°C, native enzyme Cupriavidus necator
1.1.1.103 11.6
-
 L-threonine pH 10.0, 30°C, native enzyme Cupriavidus necator

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.103 AlCl3 18% activation at 1 mM Cupriavidus necator
1.1.1.103 BaCl2 13% activation at 1 mM Cupriavidus necator
1.1.1.103 CoCl2 15% activation at 1 mM Cupriavidus necator
1.1.1.103 CrCl3 10% activation at 1 mM Cupriavidus necator
1.1.1.103 CsCl 17% activation at 1 mM Cupriavidus necator
1.1.1.103 CuSO4 15% activation at 1 mM Cupriavidus necator
1.1.1.103 MgSO4 12% activation at 1 mM Cupriavidus necator
1.1.1.103 MnSO4 12% activation at 1 mM Cupriavidus necator
1.1.1.103 additional information no effect at 1 mM by AgNO3, MgCl2, and 10 mM EDTA and ethylene glycol tetraacetic acid Cupriavidus necator
1.1.1.103 Na2MoO4 13% activation at 1 mM Cupriavidus necator
1.1.1.103 NiCl2 19% activation at 1 mM Cupriavidus necator
1.1.1.103 PbCl2 18% activation at 1 mM Cupriavidus necator
1.1.1.103 ZnSO4 9% activation at 1 mM Cupriavidus necator

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.103 34628
-
 2 x 37200, native enzyme, SDS-PAGE, x * 34628, sequence calculation Cupriavidus necator
1.1.1.103 79400
-
 native enzyme, gel filtration Cupriavidus necator

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.103 L-threonine + NAD+ Cupriavidus necator
-
 (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?
1.1.1.103 L-threonine + NAD+ Cupriavidus necator NBRC 102504
-
 (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.103 Cupriavidus necator E5RQ20
-
-
1.1.1.103 Cupriavidus necator NBRC 102504 E5RQ20
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.103 recombinant His-tagged enzyme 4.2fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, native enzyme 75.4fold by anion exchange and hydrophobic interaction chromatography, dialysis, hydroxyapatite chromatography, followed by gel filtration Cupriavidus necator

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.103 42.2
-
 purified native enzyme, pH 10.0, 30°C Cupriavidus necator
1.1.1.103 65
-
 purified recombinant enzyme, pH 10.0, 30°C Cupriavidus necator

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.103 DL-2-amino-3-hydroxyvalerate + NAD+
-
 Cupriavidus necator DL-2-amino-3-oxopentanoate + NADH + H+
-
 ?
1.1.1.103 DL-2-amino-3-hydroxyvalerate + NAD+
-
 Cupriavidus necator NBRC 102504 DL-2-amino-3-oxopentanoate + NADH + H+
-
 ?
1.1.1.103 L-threonine + NAD+
-
 Cupriavidus necator (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?
1.1.1.103 L-threonine + NAD+
-
 Cupriavidus necator NBRC 102504 (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?
1.1.1.103 additional information L-threonine and DL-2-amino-3-hydroxyvalerate are the only substrates for ThrDH among other L-amino acids, alcohols, and amino alcohols, substrate specificity, overview Cupriavidus necator ?
-
 ?
1.1.1.103 additional information L-threonine and DL-2-amino-3-hydroxyvalerate are the only substrates for ThrDH among other L-amino acids, alcohols, and amino alcohols, substrate specificity, overview Cupriavidus necator NBRC 102504 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.103 dimer 2 x 37200, native enzyme, SDS-PAGE, x * 34628, sequence calculation Cupriavidus necator

Synonyms

EC Number Synonyms Comment Organism
1.1.1.103 ThrDH
-
 Cupriavidus necator

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.103 75
-
-
 Cupriavidus necator

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.103 25 80 activity range, profile overview Cupriavidus necator

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.103 25 75 quite stable at, rapid loss of activity above 80°C Cupriavidus necator

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.103 38
-
 NAD+ pH 10.0, 30°C, native enzyme Cupriavidus necator
1.1.1.103 43.8
-
 L-threonine pH 10.0, 30°C, native enzyme Cupriavidus necator

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.103 10
-
 glycine-KOH buffer Cupriavidus necator

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.103 6 12 activity range, pH-dependent activity varies in different buffer systems, profile overview Cupriavidus necator

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.103 4 11 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 Cupriavidus necator

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.103 NAD+ dependent on Cupriavidus necator

General Information

EC Number General Information Comment Organism
1.1.1.103 evolution the enzyme belongs to the extended short-chain alcohol dehydrogenase superfamily Cupriavidus necator
1.1.1.103 additional information the enzyme possesses a glycine-rich NAD+-binding domain at the N terminus and conserved catalytic triad of YxxxK residues Cupriavidus necator