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Literature summary for 1.1.1.103 extracted from

  • Shimizu, Y.; Sakuraba, H.; Kawakami, R.; Goda, S.; Kawarabayasi, Y.; Ohshima, T.
    L-Threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3: gene cloning and enzymatic characterization (2005), Extremophiles, 9, 317-324.
    View publication on PubMed
Search for more literature for 1.1.1.103

Cloned(Commentary)

Cloned (Comment) Organism
orf PH0655, amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain TOP10 Pyrococcus horikoshii

Inhibitors

Inhibitors Comment Organism Structure
L-2-amino-3-oxobutyrate competitive product inhibition by the unstable L-2-amino-3-oxobutyrate only in presence of NADH, which stabilizes Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can replace Zn2+ with 35% of the activity with Zn2+ Pyrococcus horikoshii
Mn2+ can replace Zn2+ with 77% of the activity with Zn2+ Pyrococcus horikoshii
Zn2+ required Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41200
-
 4 * 41200, recombinant enzyme, SDS-PAGE, 4 * 41815, sequence calculation Pyrococcus horikoshii
41815
-
 4 * 41200, recombinant enzyme, SDS-PAGE, 4 * 41815, sequence calculation Pyrococcus horikoshii
192000
-
 recombinant enzyme, gel filtration Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-threonine + NAD+ Pyrococcus horikoshii
-
 (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?
L-threonine + NAD+ Pyrococcus horikoshii OT-3
-
 (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii
-
 strain OT3
-
Pyrococcus horikoshii OT-3
-
 strain OT3
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain TOP10 by nickel affinity chromatography Pyrococcus horikoshii

Reaction

Reaction Comment Organism Reaction ID
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+ reaction mechanism, random bi bi kinetic mechanism Pyrococcus horikoshii
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.43
-
 purified recombinant enzyme Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DL-threo-3-phenylserine + NAD+ 53% of the activity with L-threonine Pyrococcus horikoshii ? + NADH
-
 ?
DL-threo-3-phenylserine + NAD+ 53% of the activity with L-threonine Pyrococcus horikoshii OT-3 ? + NADH
-
 ?
L-serine + NAD+ 21% of the activity with L-threonine Pyrococcus horikoshii ? + NADH
-
 ?
L-serine + NAD+ 21% of the activity with L-threonine Pyrococcus horikoshii OT-3 ? + NADH
-
 ?
L-threonine + NAD+
-
 Pyrococcus horikoshii (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?
L-threonine + NAD+ stereospecificity, overview Pyrococcus horikoshii (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?
L-threonine + NAD+
-
 Pyrococcus horikoshii OT-3 (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?
L-threonine + NAD+ stereospecificity, overview Pyrococcus horikoshii OT-3 (2S)-2-amino-3-oxobutanoate + NADH + H+
-
 ?
additional information substrate specificity, overview Pyrococcus horikoshii ?
-
 ?
additional information substrate specificity, overview Pyrococcus horikoshii OT-3 ?
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 41200, recombinant enzyme, SDS-PAGE, 4 * 41815, sequence calculation Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
L-ThrDH
-
 Pyrococcus horikoshii
L-threonine dehydrogenase
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
 Pyrococcus horikoshii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
 60 min, pH 7.0, over 90% remaining activity, purified recombinant enzyme Pyrococcus horikoshii
100
-
 30 min, pH 7.0, over 90% remaining activity, purified recombinant enzyme Pyrococcus horikoshii
105
-
 higher loss of activity above, purified recombinant enzyme Pyrococcus horikoshii
120
-
 20 min, inactivation, purified recombinant enzyme Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
 Pyrococcus horikoshii

pH Range

pH Minimum pH Maximum Comment Organism
9.2 12 22% of maximal activity at pH 9.2, 50% at pH 9.5, and 52% at pH 12.0 Pyrococcus horikoshii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Pyrococcus horikoshii